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佐々木卓也

徳島大学

プロフィール
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リサーチマップ・
Jグローバル
KAKEN
注目研究

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2024年4月1日更新

職名: 理事
電話: 088-633-9223
電子メール: sasaki@basic.med.tokushima-u.ac.jp
学歴: 1985/3: 神戸大学医学部卒業
1991/3: 神戸大学大学院医学研究科修了(医博修了)
学位: 医学博士 (神戸大学) (1991年3月)
職歴・経歴: 1985/12: 兵庫県立こども病院医員
1986/4: 国家公務員等共済組合連合会呉共済病院医員
1992/1: 神戸大学助手医学部
1994/4: 大阪大学助手医学部
1998/10: 大阪大学助教授医学部
2000/4: 徳島大学教授医学部
2002/4: 徳島大学教授大学院医学研究科
2004/4: 徳島大学教授大学院ヘルスパイオサイエンス研究部

専門分野・研究分野: 生化学 (Biochemistry)
分子生物学 (Molecular Biology)
細胞生物学 (Cell Biology)

研究者総覧で最新データを確認する

2024年4月1日更新

専門分野・研究分野: 生化学 (Biochemistry)
分子生物学 (Molecular Biology)
細胞生物学 (Cell Biology)
担当経験のある授業科目: 先端医学 (学部)
医学概論 (共通教育)
基礎医学 (学部)
基礎医学統合実習 (学部)
基礎医学統合実習(生化学) (学部)
基礎医学統合実習(生理学) (学部)
基礎医学統合実習(薬理学:2年) (学部)
技術英語入門 (学部)
生体制御医学実験実習・臨床研究実習 (大学院)
生化学 (大学院)
生化学・生化学実習 (学部)
生化学入門 (共通教育)
生化学実習 (学部)
生化学演習 (大学院)
研究室配属 (学部)
指導経験: 研究者総覧に該当データはありませんでした。

研究者総覧で最新データを確認する

2024年4月1日更新

専門分野・研究分野: 生化学 (Biochemistry)
分子生物学 (Molecular Biology)
細胞生物学 (Cell Biology)

研究テーマ: 小胞輸送ならびに細胞骨格の制御機構
神経機能異常や癌の浸潤·転移等の病態の解明をターゲットにしている (細胞内シグナル伝達, 神経伝達物質放出, 記憶形成, 細胞運動, 細胞接着)

著書

Ayuko Sakane and Takuya Sasaki :
Roles of Rab family small G proteins in formation of the apical junctional complex in epithelial cells.,
Cell Polarity: Biological Role and Basic Mechanisms, Germany, Feb. 2015.

(出版サイトへのリンク): ● Publication site (DOI): 10.1007/978-3-319-14463-4_15
(文献検索サイトへのリンク): ● Search Scopus @ Elsevier (DOI): 10.1007/978-3-319-14463-4_15

(DOI: 10.1007/978-3-319-14463-4_15) H. Nakanishi, Takuya Sasaki, J. Miyoshi and Y. Takai :
Rab3A small G protein and its regulators in neurotransmitter release and synaptic plasticity.,
2002. S. Orita, Takuya Sasaki and Y. Takai :
Doc2 as a presynaptic modulator for neurotransmitter releas.,
Springer-Verlag Tokyo Inc., 1999. Takuya Sasaki, K. Tanaka, K. Takaishi, K. Takahashi and Y. Takai :
The Rho family-Rho GDI system as a temporal and spatial determinant for cytoskeletal control.,
Hokkaido University School of Medicine, 1998. Takuya Sasaki, H. Shirataki, H. Nakanishi and Y. Takai :
Rab3A-rabphilin-3A system in neurotransmitter release.,
Lippincott-Raven Publishers, USA, 1997. H. Shirataki, Takuya Sasaki and Y. Takai :
Mode of action of Rab3A system in neurotransmitter release.,
Elsevier Science, Amsterdam, 1996. K. Tanaka, A. Kikuchi, K. Kaibuchi, Takuya Sasaki and Y. Takai :
Rho GDI,
Oxford University Press, 1995. Takuya Sasaki, A. Kikuchi, K. Kaibuchi and Y. Takai :
Rab GDI,
Oxford University Press, 1995. 織田聡, 佐々木卓也, 高井義美 :
RasとRhoの機能と作用機構,
株式会社メジカルビュー社, 1994年. Y. Takai, K. Kaibuchi, A. Kikuchi, Takuya Sasaki, H. Shirataki and K. Tanaka :
Function and mode of action of small G protein.,
John Willy & Sons, Inc., 1994. Y. Takai, K. Kaibuchi, Takuya Sasaki, K. Tanaka, H. Shirataki and H. Nakanishi :
Rho small G protein and cytoskeletal control,
Princeton Scientific Publishing Co., Inc., 1994. Yoshimi Takai, Kozo Kaibuchi, Akira Kikuchi, Takuya Sasaki and Hiromichi Shirataki :
Regulators of small GTPases.,
John Wiley & Sons, Inc., Chichester, 1993. Yoshimi Takai, Kozo Kaibuchi, Akira Kikuchi, M. Kawata, Takuya Sasaki and T. Yamamoto :
GDP/GTP exchange proteins for small GTP-binding proteins.,
CRC press, Boca Raton, 1993. Yoshimi Takai, Kozo Kaibuchi, Akira Kikuchi and Takuya Sasaki :
GDP/GTP exchange proteins for small GTP-binding proteins.,
Springer-Verlag GmbH & Co., Heidelberg, 1993.

論文

Taira Kajisa, Taka-aki Yano, Hidenori Koresawa, Kunihiro Otsuka, Ayuko Sakane, Takuya Sasaki, Koji Yasutomo and Takeshi Yasui :
Highly sensitive detection of nucleocapsid protein from SARS-CoV-2 using a near-infrared surface plasmon resonance sensing system,
Optics Continuum, Vol.11, No.1, 2336-2346, 2022.

(出版サイトへのリンク): ● Publication site (DOI): 10.1364/OPTCON.472486
(文献検索サイトへのリンク): ● Search Scopus @ Elsevier (DOI): 10.1364/OPTCON.472486

(DOI: 10.1364/OPTCON.472486) Taka-aki Yano, Taira Kajisa, Masayuki Ono, Yoshiya Miyasaka, Yuichi Hasegawa, Atsushi Saito, Kunihiro Otsuka, Ayuko Sakane, Takuya Sasaki, Koji Yasutomo, Rina Hamajima, Yuta Kanai, Takeshi Kobayashi, Yoshiharu Matsuura, Makoto Itonaga and Takeshi Yasui :
Ultrasensitive detection of SARS-CoV-2 nucleocapsid protein using large gold nanoparticle-enhanced surface plasmon resonance.,
Scientific Reports, Vol.12, No.1, 1060, 2022.

(要約): The COVID-19 pandemic has created urgent demand for rapid detection of the SARS-CoV-2 coronavirus. Herein, we report highly sensitive detection of SARS-CoV-2 nucleocapsid protein (N protein) using nanoparticle-enhanced surface plasmon resonance (SPR) techniques. A crucial plasmonic role in significantly enhancing the limit of detection (LOD) is revealed for exceptionally large gold nanoparticles (AuNPs) with diameters of hundreds of nm. SPR enhanced by these large nanoparticles lowered the LOD of SARS-CoV-2 N protein to 85 fM, resulting in the highest SPR detection sensitivity ever obtained for SARS-CoV-2 N protein.
(キーワード): Coronavirus Nucleocapsid Proteins / Gold / Metal Nanoparticles / Phosphoproteins / SARS-CoV-2 / Surface Plasmon Resonance
(徳島大学機関リポジトリ): ● Metadata: 117264
(出版サイトへのリンク): ● Publication site (DOI): 10.1038/s41598-022-05036-x
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 35058513; ● Search Scopus @ Elsevier (PMID): 35058513; ● Search Scopus @ Elsevier (DOI): 10.1038/s41598-022-05036-x

(徳島大学機関リポジトリ: 117264, DOI: 10.1038/s41598-022-05036-x, PubMed: 35058513) Ayuko Sakane, Taka-aki Yano, Takayuki Uchihashi, Kazuki Horikawa, Yusuke Hara, Issei Imoto, Shusaku Kurisu, Hiroshi Yamada, Kohji Takei and Takuya Sasaki :
JRAB/MICAL-L2 undergoes liquid-liquid phase separation to form tubular recycling endosomes.,
Communications Biology, Vol.4, No.1, 551, 2021.

(要約): Elongated tubular endosomes play essential roles in diverse cellular functions. Multiple molecules have been implicated in tubulation of recycling endosomes, but the mechanism of endosomal tubule biogenesis has remained unclear. In this study, we found that JRAB/MICAL-L2 induces endosomal tubulation via activated Rab8A. In association with Rab8A, JRAB/MICAL-L2 adopts its closed form, which functions in the tubulation of recycling endosomes. Moreover, JRAB/MICAL-L2 induces liquid-liquid phase separation, initiating the formation of tubular recycling endosomes upon overexpression. Between its N-terminal and C-terminal globular domains, JRAB/MICAL-L2 contains an intrinsically disordered region, which contributes to the formation of JRAB/MICAL-L2 condensates. Based on our findings, we propose that JRAB/MICAL-L2 plays two sequential roles in the biogenesis of tubular recycling endosomes: first, JRAB/MICAL-L2 organizes phase separation, and then the closed form of JRAB/MICAL-L2 formed by interaction with Rab8A promotes endosomal tubulation.
(徳島大学機関リポジトリ): ● Metadata: 117215
(出版サイトへのリンク): ● Publication site (DOI): 10.1038/s42003-021-02080-7
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 33976349; ● Search Scopus @ Elsevier (PMID): 33976349; ● Search Scopus @ Elsevier (DOI): 10.1038/s42003-021-02080-7

(徳島大学機関リポジトリ: 117215, DOI: 10.1038/s42003-021-02080-7, PubMed: 33976349) The Mon La, Hiromi Tachibana, Shun-Ai Li, Tadashi Abe, Sayaka Seiriki, Hikaru Nagaoka, Eizo Takashima, Tetsuya Takeda, Daisuke Ogawa, Shin-Ichi Makino, Katsuhiko Asanuma, Masami Watanabe, Xuefei Tian, Shuta Ishibe, Ayuko Sakane, Takuya Sasaki, Jun Wada, Kohji Takei and Hiroshi Yamada :
Dynamin 1 is important for microtubule organization and stabilization in glomerular podocytes.,
The FASEB journal, Vol.34, No.12, 16449-16463, 2020.

(要約): Dynamin 1 is a neuronal endocytic protein that participates in vesicle formation by scission of invaginated membranes. Dynamin 1 is also expressed in the kidney; however, its physiological significance to this organ remains unknown. Here, we show that dynamin 1 is crucial for microtubule organization and stabilization in glomerular podocytes. By immunofluorescence and immunoelectron microscopy, dynamin 1 was concentrated at microtubules at primary processes in rat podocytes. By immunofluorescence of differentiated mouse podocytes (MPCs), dynamin 1 was often colocalized with microtubule bundles, which radially arranged toward periphery of expanded podocyte. In dynamin 1-depleted MPCs by RNAi, α-tubulin showed a dispersed linear filament-like localization, and microtubule bundles were rarely observed. Furthermore, dynamin 1 depletion resulted in the formation of discontinuous, short acetylated α-tubulin fragments, and the decrease of microtubule-rich protrusions. Dynamins 1 and 2 double-knockout podocytes showed dispersed acetylated α-tubulin and rare protrusions. In vitro, dynamin 1 polymerized around microtubules and cross-linked them into bundles, and increased their resistance to the disassembly-inducing reagents Ca and podophyllotoxin. In addition, overexpression and depletion of dynamin 1 in MPCs increased and decreased the nocodazole resistance of microtubules, respectively. These results suggest that dynamin 1 supports the microtubule bundle formation and participates in the stabilization of microtubules.
(キーワード): Animals / Cells, Cultured / Dynamin I / Endocytosis / Epithelial Cells / Kidney / 男性 (male) / Mice / Mice, Inbred C57BL / ノックアウトマウス (knockout mice) / Microtubule-Associated Proteins / Microtubules / Podocytes / Rats / Tubulin
(出版サイトへのリンク): ● Publication site (DOI): 10.1096/fj.202001240RR
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 33070431; ● Summary page in Scopus @ Elsevier: 2-s2.0-85092620747

(DOI: 10.1096/fj.202001240RR, PubMed: 33070431, Elsevier: Scopus) Shotaro Sakakibara, Kiyohito Mizutani, Ayumu Sugiura, Ayuko Sakane, Takuya Sasaki, Shigenobu Yonemura and Yoshimi Takai :
Afadin regulates actomyosin organization through αE-catenin at adherens junctions.,
The Journal of Cell Biology, Vol.219, No.5, 2020.

(要約): Actomyosin-undercoated adherens junctions are critical for epithelial cell integrity and remodeling. Actomyosin associates with adherens junctions through αE-catenin complexed with β-catenin and E-cadherin in vivo; however, in vitro biochemical studies in solution showed that αE-catenin complexed with β-catenin binds to F-actin less efficiently than αE-catenin that is not complexed with β-catenin. Although a "catch-bond model" partly explains this inconsistency, the mechanism for this inconsistency between the in vivo and in vitro results remains elusive. We herein demonstrate that afadin binds to αE-catenin complexed with β-catenin and enhances its F-actin-binding activity in a novel mechanism, eventually inducing the proper actomyosin organization through αE-catenin complexed with β-catenin and E-cadherin at adherens junctions.
(徳島大学機関リポジトリ): ● Metadata: 115835
(出版サイトへのリンク): ● Publication site (DOI): 10.1083/jcb.201907079
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 32227204; ● Search Scopus @ Elsevier (PMID): 32227204; ● Search Scopus @ Elsevier (DOI): 10.1083/jcb.201907079

(徳島大学機関リポジトリ: 115835, DOI: 10.1083/jcb.201907079, PubMed: 32227204) Kazuhisa Miyake, Ayuko Sakane, Ikuko Sagawa, Yoko Tomida, Jiro Kasahara and Takuya Sasaki :
Actin Cytoskeletal Reorganization Function of JRAB/MICAL-L2 Is Fine-tuned by Intramolecular Interaction between First LIM Zinc Finger and C-terminal Coiled-coil Domains,
Scientific Reports, Vol.9, No.1, 12794, 2019.

(要約): JRAB/MICAL-L2 is an effector protein of Rab13, a member of the Rab family of small GTPase. JRAB/MICAL-L2 consists of a calponin homology domain, a LIM domain, and a coiled-coil domain. JRAB/MICAL-L2 engages in intramolecular interaction between the N-terminal LIM domain and the C-terminal coiled-coil domain, and changes its conformation from closed to open under the effect of Rab13. Open-form JRAB/MICAL-L2 induces the formation of peripheral ruffles via an interaction between its calponin homology domain and filamin. Here, we report that the LIM domain, independent of the C-terminus, is also necessary for the function of open-form JRAB/MICAL-L2. In mechanistic terms, two zinc finger domains within the LIM domain bind the first and second molecules of actin at the minus end, potentially inhibiting the depolymerization of actin filaments (F-actin). The first zinc finger domain also contributes to the intramolecular interaction of JRAB/MICAL-L2. Moreover, the residues of the first zinc finger domain that are responsible for the intramolecular interaction are also involved in the association with F-actin. Together, our findings show that the function of open-form JRAB/MICAL-L2 mediated by the LIM domain is fine-tuned by the intramolecular interaction between the first zinc finger domain and the C-terminal domain.
(キーワード): 3T3 Cells / Actins / Animals / Cytoskeleton / Hydrogen Deuterium Exchange-Mass Spectrometry / Mice / Microfilament Proteins / Models, Molecular / Mutation / Protein Domains / 構造活性相関 (structureactivity relationship) / Zinc Fingers
(徳島大学機関リポジトリ): ● Metadata: 114610
(出版サイトへのリンク): ● Publication site (DOI): 10.1038/s41598-019-49232-8
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 31488862; ● Summary page in Scopus @ Elsevier: 2-s2.0-85071764631

(徳島大学機関リポジトリ: 114610, DOI: 10.1038/s41598-019-49232-8, PubMed: 31488862, Elsevier: Scopus) Ryuta Nomiyama, Masahiro Emoto, Naofumi Fukuda, Kumiko Matsui, Manabu Kondo, Ayuko Sakane, Takuya Sasaki and Yukio Tanizawa :
Protein kinase C iota facilitates insulin-induced glucose transport by phosphorylation of soluble nSF attachment protein receptor regulator (SNARE) double C2 domain protein b.,
Journal of Diabetes Investigation, Vol.10, No.3, 591-601, 2019.

(要約): Double C2 domain protein b (DOC2b), one of the synaptotagmins, has been shown to translocate to the plasma membrane, and to initiate membrane-fusion processes of vesicles containing glucose transporter 4 proteins on insulin stimulation. However, the mechanism by which DOC2b is regulated remains unclear. Herein, we identified the upstream regulatory factors of DOC2b in insulin signal transduction. We also examined the role of DOC2b on systemic homeostasis using DOC2b knockout (KO) mice. We first identified DOC2b binding proteins by immunoprecipitation and mutagenesis experiments. Then, DOC2b KO mice were generated by disrupting the first exon of the DOC2b gene. In addition to the histological examination, glucose metabolism was assessed by measuring parameters on glucose/insulin tolerance tests. Insulin-stimulated glucose uptake was also measured using isolated soleus muscle and epididymal adipose tissue. We identified an isoform of atypical protein kinase C (protein kinase C iota) that can bind to DOC2b and phosphorylates one of the serine residues of DOC2b (S34). This phosphorylation is essential for DOC2b translocation. DOC2b KO mice showed insulin resistance and impaired oral glucose tolerance on insulin and glucose tolerance tests, respectively. Insulin-stimulated glucose uptake was impaired in isolated soleus muscle and epididymal adipose tissues from DOC2b KO mice. We propose a novel insulin signaling mechanism by which protein kinase C iota phosphorylates DOC2b, leading to glucose transporter 4 vesicle translocation, fusion and facilitation of glucose uptake in response to insulin. The present results also showed DOC2b to play important roles in systemic glucose homeostasis.
(キーワード): 3T3-L1 Cells / Adipocytes / Animals / Calcium-Binding Proteins / Cells, Cultured / グルコース (glucose) / Glucose Intolerance / Hypoglycemic Agents / インスリン (insulin) / インスリン抵抗性 (insulin resistance) / Islets of Langerhans / Isoenzymes / 男性 (male) / Mice / Mice, Inbred C57BL / ノックアウトマウス (knockout mice) / Muscle, Skeletal / Nerve Tissue Proteins / リン酸化 (phosphorylation) / Protein Kinase C
(徳島大学機関リポジトリ): ● Metadata: 116748
(出版サイトへのリンク): ● Publication site (DOI): 10.1111/jdi.12965
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 30369065; ● Summary page in Scopus @ Elsevier: 2-s2.0-85057793668

(徳島大学機関リポジトリ: 116748, DOI: 10.1111/jdi.12965, PubMed: 30369065, Elsevier: Scopus) Tomohiko Maruo, Shotaro Sakakibara, Muneaki Miyata, Yu Itoh, Souichi Kurita, Kenji Mandai, Takuya Sasaki and Yoshimi Takai :
Involvement of l-afadin, but not s-afadin, in the formation of puncta adherentia junctions of hippocampal synapses.,
Molecular and Cellular Neuroscience, Vol.92, 40-49, 2018.

(要約): A hippocampal mossy fiber synapse has a complex structure in which presynaptic boutons attach to the dendritic trunk by puncta adherentia junctions (PAJs) and wrap multiply-branched spines, forming synaptic junctions. It was previously shown that afadin regulates the formation of the PAJs cooperatively with nectin-1, nectin-3, and N-cadherin. Afadin is a nectin-binding protein with two splice variants, l-afadin and s-afadin: l-afadin has an actin filament-binding domain, whereas s-afadin lacks it. It remains unknown which variant is involved in the formation of the PAJs or how afadin regulates it. We showed here that re-expression of l-afadin, but not s-afadin, in the afadin-deficient cultured hippocampal neurons in which the PAJ-like structure was disrupted, restored this structure as estimated by the accumulation of N-cadherin and αΝ-catenin. The l-afadin mutant, in which the actin filament-binding domain was deleted, or the l-afadin mutant, in which the αΝ-catenin-binding domain was deleted, did not restore the PAJ-like structure. These results indicate that l-afadin, but not s-afadin, regulates the formation of the hippocampal synapse PAJ-like structure through the binding to actin filaments and αN-catenin. We further found here that l-afadin bound αN-catenin, but not γ-catenin, whereas s-afadin bound γ-catenin, but hardly αN-catenin. These results suggest that the inability of s-afadin to form the hippocampal synapse PAJ-like structure is due to its inability to efficiently bind αN-catenin.
(キーワード): Actins / Adherens Junctions / Animals / Binding Sites / Catenins / Cells, Cultured / 男性 (male) / Mice / Mice, Inbred C57BL / Mice, Inbred ICR / Microfilament Proteins / Mossy Fibers, Hippocampal / Protein Binding / Protein Isoforms / Synapses
(出版サイトへのリンク): ● Publication site (DOI): 10.1016/j.mcn.2018.06.006
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 29969655; ● Summary page in Scopus @ Elsevier: 2-s2.0-85049558291

(DOI: 10.1016/j.mcn.2018.06.006, PubMed: 29969655, Elsevier: Scopus) Ayuko Sakane, Shin Yoshizawa, Hideo Yokota and Takuya Sasaki :
Dancing Styles of Collective Cell Migration: Image-Based Computational Analysis of JRAB/MICAL-L2.,
Frontiers in Cell and Developmental Biology, Vol.6, 4, 2018.

(要約): Collective cell migration is observed during morphogenesis, angiogenesis, and wound healing, and this type of cell migration also contributes to efficient metastasis in some kinds of cancers. Because collectively migrating cells are much better organized than a random assemblage of individual cells, there seems to be a kind of order in migrating clusters. Extensive research has identified a large number of molecules involved in collective cell migration, and these factors have been analyzed using dramatic advances in imaging technology. To date, however, it remains unclear how myriad cells are integrated as a single unit. Recently, we observed unbalanced collective cell migrations that can be likened to either precision dancing or , Japanese traditional dancing similar to the style at Rio Carnival, caused by the impairment of the conformational change of JRAB/MICAL-L2. This review begins with a brief history of image-based computational analyses on cell migration, explains why quantitative analysis of the stylization of collective cell behavior is difficult, and finally introduces our recent work on JRAB/MICAL-L2 as a successful example of the multidisciplinary approach combining cell biology, live imaging, and computational biology. In combination, these methods have enabled quantitative evaluations of the "dancing style" of collective cell migration.
(徳島大学機関リポジトリ): ● Metadata: 116728
(出版サイトへのリンク): ● Publication site (DOI): 10.3389/fcell.2018.00004
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 29468157; ● Summary page in Scopus @ Elsevier: 2-s2.0-85042102406

(徳島大学機関リポジトリ: 116728, DOI: 10.3389/fcell.2018.00004, PubMed: 29468157, Elsevier: Scopus) Ayuko Sakane, Shin Yoshizawa, Masaomi Nishimura, Yuko Tsuchiya, Natsuki Matsushita, Kazuhisa Miyake, Kazuki Horikawa, Issei Imoto, Chiharu Mizuguchi, Hiroyuki Saito, Takato Ueno, Sachi Matsushita, Hisashi Haga, Shinji Deguchi, Kenji Mizuguchi, Hideo Yokota and Takuya Sasaki :
Conformational plasticity of JRAB/MICAL-L2 provides "law and order" in collective cell migration.,
Molecular Biology of the Cell, Vol.27, No.20, 3095-3108, 2016.

(要約): In fundamental biological processes, cells often move in groups, a process termed collective cell migration. Collectively migrating cells are much better organized than a random assemblage of individual cells. Many molecules have been identified as factors involved in collective cell migration, and no one molecule is adequate to explain the whole picture. Here we show that JRAB/MICAL-L2, an effector protein of Rab13 GTPase, provides the "law and order" allowing myriad cells to behave as a single unit just by changing its conformation. First, we generated a structural model of JRAB/MICAL-L2 by a combination of bioinformatic and biochemical analyses and showed how JRAB/MICAL-L2 interacts with Rab13 and how its conformational change occurs. We combined cell biology, live imaging, computational biology, and biomechanics to show that impairment of conformational plasticity in JRAB/MICAL-L2 causes excessive rigidity and loss of directionality, leading to imbalance in cell group behavior. This multidisciplinary approach supports the concept that the conformational plasticity of a single molecule provides "law and order" in collective cell migration.
(キーワード): Actinin / Animals / Cell Movement / Computational Biology / Dogs / Epithelial Cells / Focal Adhesions / HEK293 Cells / Humans / Madin Darby Canine Kidney Cells / Microfilament Proteins / Optical Imaging / Protein Binding / Protein Structure, Tertiary / Protein Transport / Tight Junctions / rab GTP-Binding Proteins
(徳島大学機関リポジトリ): ● Metadata: 114562
(出版サイトへのリンク): ● Publication site (DOI): 10.1091/mbc.E16-05-0332
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 27582384; ● Search Scopus @ Elsevier (PMID): 27582384; ● Search Scopus @ Elsevier (DOI): 10.1091/mbc.E16-05-0332

(徳島大学機関リポジトリ: 114562, DOI: 10.1091/mbc.E16-05-0332, PubMed: 27582384) Ayuko Sakane, Ahmed Mahmoud Alamir Abdallah, Kiyoshi Nakano, Kazufumi Honda, Toshio Kitamura, Issei Imoto, Natsuki Matsushita and Takuya Sasaki :
Junctional Rab13-binding protein (JRAB) regulates cell spreading via filamins.,
Genes to Cells, Vol.18, No.9, 810-822, 2013.

(要約): We previously showed that Rab13 and its effector protein, junctional Rab13-binding protein (JRAB)/molecules interacting with CasL-like 2 (MICAL-L2), regulate junctional development by modulating cell adhesion molecule transport and actin cytoskeletal reorganization in epithelial cells. Here, we investigated how JRAB regulates reorganization of the actin cytoskeleton in NIH3T3 fibroblasts, in an attempt to obtain novel insights into the mechanism of JRAB action. To this end, we expressed mutant proteins that adopt a constitutively open or closed state and then examined effect on cellular morphology of the resulting actin cytoskeletal reorganization. Expression of the JRABΔCT mutant (constitutively 'closed' state) induced stress fibers, whereas expression of the JRABΔCC mutant (constitutively 'open' state) caused cell spreading with membrane ruffles. Next, we identified the proteins involved in JRAB-induced rearrangement of actin cytoskeleton leading to morphological changes. In NIH3T3 cells expressing HA-JRABΔCC, filamin, an actin cross-linking protein, coimmunoprecipitated with HA-JRABΔCC. Expression of ASB2 induced degradation of all three filamin isoforms and inhibited the JRABΔCC-induced cell spreading. Consistent with our previous results, actinin-1/-4 were also immunoprecipitated with HA-JRABΔCC. However, actinin-1/-4 have no effect on the cell spreading regulated by JRABΔCC. These data suggest that JRAB contributes to the rearrangement of the actin cytoskeleton during cell spreading via filamins.
(キーワード): Actinin / Animals / Cell Membrane / Cytoskeletal Proteins / Filamins / HEK293 Cells / Humans / Mice / Mutation / NIH 3T3 Cells / Protein Binding / Protein Isoforms / Protein Structure, Tertiary / Stress Fibers
(徳島大学機関リポジトリ): ● Metadata: 105908
(出版サイトへのリンク): ● Publication site (DOI): 10.1111/gtc.12078
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 23890175; ● Summary page in Scopus @ Elsevier: 2-s2.0-84883173734

(徳島大学機関リポジトリ: 105908, DOI: 10.1111/gtc.12078, PubMed: 23890175, Elsevier: Scopus) Ayuko Sakane, Ahmed Alamir Mahmoud Abdallah, Kiyoshi Nakano, Kazufumi Honda, Wataru Ikeda, Yumiko Nishikawa, Mitsuru Matsumoto, Natsuki Matsushita, Toshio Kitamura and Takuya Sasaki :
Rab13 small G protein and junctional Rab13-binding protein (JRAB) orchestrate actin cytoskeletal organization during epithelial junctional development.,
The Journal of Biological Chemistry, Vol.287, No.51, 42455-42468, 2012.

(要約): During epithelial junctional development, both vesicle transport and reorganization of the actin cytoskeleton must be spatiotemporally regulated. Coordination of these cellular functions is especially important, but the precise mechanism remains elusive. Previously, we identified junctional Rab13-binding protein (JRAB)/molecules interacting with CasL-like 2 (MICAL-L2) as an effector of the Rab13 small G protein, and we found that the Rab13-JRAB system may be involved in the formation of cell-cell adhesions via transport of adhesion molecules. Here, we showed that JRAB interacts with two actin-binding proteins, actinin-1 and -4, and filamentous actin via different domains and regulates actin cross-linking and stabilization through these interactions. During epithelial junctional development, JRAB is prominently enriched in the actin bundle at the free border; subsequently, JRAB undergoes a Rab13-dependent conformational change that is required for maturation of cell-cell adhesion sites. These results suggest that Rab13 and JRAB regulate reorganization of the actin cytoskeleton throughout epithelial junctional development from establishment to maturation of cell-cell adhesion.
(キーワード): Actin Cytoskeleton / Actinin / Actins / Animals / Cell Line / Cell Membrane / Cytoskeletal Proteins / Epithelial Cells / Epithelium / Humans / Mice / Models, Biological / Protein Binding / Protein Multimerization / Protein Structure, Tertiary / Protein Transport / Tight Junctions / rab GTP-Binding Proteins
(出版サイトへのリンク): ● Publication site (DOI): 10.1074/jbc.M112.383653
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 23100251; ● Search Scopus @ Elsevier (PMID): 23100251; ● Search Scopus @ Elsevier (DOI): 10.1074/jbc.M112.383653

(DOI: 10.1074/jbc.M112.383653, PubMed: 23100251) Kanchanamala Withanage, Kentaro Nakagawa, Mitsunobu Ikeda, Hidetake Kurihara, Takumi Kudo, Zeyu Yang, Ayuko Sakane, Takuya Sasaki and Yutaka Hata :
Expression of RASSF6 in kidney and the implication of RASSF6 and the Hippo pathway in the sorbitol-induced apoptosis in renal proximal tubular epithelial cells.,
The Journal of Biochemistry, Vol.152, No.1, 111-119, 2012.

(要約): RASSF6, a member of RASSF tumour suppressor proteins, binds to mammalian Ste20-like kinases (MST1/2), core kinases of the proapoptotic Hippo pathway and cooperates with the Hippo pathway to induce apoptosis. We originally identified RASSF6 as a putative interactor of membrane-associated guanylate kinase inverted (MAGI)-1 by the yeast two-hybrid screening. We used human kidney cDNA library for the screening. MAGI-1 is abundantly expressed in kidney and is a core component of the slit diaphragm. These findings suggest that RASSF6 is expressed in kidney. However, the function of RASSF6 in kidney is not yet studied. We performed this study to confirm the interaction of RASSF6 with MAGI-1, to analyse the expression of RASSF6 in kidney and to gain insight into the function of RASSF6 in kidney. RASSF6 binds to PDZ domains of MAGI-1 through its C-terminal PDZ-binding motif and is coimmunoprecipitated with MAGI-1 from rat liver. RASSF6 is localized in normal kidney glomerulus but disappears when the slit diaphragm is disrupted in nephrotic kidney. RASSF6 is also localized on apical membranes in renal proximal tubular epithelial cells. We demonstrated that RASSF6 as well as the Hippo pathway are involved in the sorbitol-induced apoptosis in immortalized human proximal renal tubular epithelial HK-2 cells.
(キーワード): Animals / Apoptosis / Cell Line / Epithelial Cells / HEK293 Cells / Humans / Kidney / Kidney Tubules, Proximal / Male / Microscopy, Fluorescence / Monomeric GTP-Binding Proteins / PDZ Domains / Protein-Serine-Threonine Kinases / Rats / Signal Transduction / Sorbitol
(出版サイトへのリンク): ● Publication site (DOI): 10.1093/jb/mvs056
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 22577168; ● Search Scopus @ Elsevier (PMID): 22577168; ● Search Scopus @ Elsevier (DOI): 10.1093/jb/mvs056

(DOI: 10.1093/jb/mvs056, PubMed: 22577168) Keisuke Tabata, Kohichi Matsunaga, Ayuko Sakane, Takuya Sasaki, Takeshi Noda and Tamotsu Yoshimori :
Rubicon and PLEKHM1 negatively regulate the endocytic/autophagic pathway via a novel Rab7-binding domain.,
Molecular Biology of the Cell, Vol.21, No.23, 4162-4173, 2010.

(要約): The endocytic and autophagic pathways are involved in the membrane trafficking of exogenous and endogenous materials to lysosomes. However, the mechanisms that regulate these pathways are largely unknown. We previously reported that Rubicon, a Beclin 1-binding protein, negatively regulates both the autophagic and endocytic pathways by unidentified mechanisms. In this study, we performed database searches to identify potential Rubicon homologues that share the common C-terminal domain, termed the RH domain. One of them, PLEKHM1, the causative gene of osteopetrosis, also suppresses endocytic transport but not autophagosome maturation. Rubicon and PLEKHM1 specifically and directly interact with Rab7 via their RH domain, and this interaction is critical for their function. Furthermore, we show that Rubicon but not PLEKHM1 uniquely regulates membrane trafficking via simultaneously binding both Rab7 and PI3-kinase.
(キーワード): Adaptor Proteins, Signal Transducing / Apoptosis Regulatory Proteins / Autophagy / Endocytosis / HeLa Cells / Humans / Immunoblotting / Intracellular Signaling Peptides and Proteins / Lysosomes / Membrane Glycoproteins / Membrane Proteins / Membrane Transport Modulators / Microscopy, Fluorescence / Phosphatidylinositol 3-Kinases / Protein Interaction Domains and Motifs / Protein Transport / rab GTP-Binding Proteins
(出版サイトへのリンク): ● Publication site (DOI): 10.1091/mbc.E10-06-0495
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 20943950; ● Search Scopus @ Elsevier (PMID): 20943950; ● Search Scopus @ Elsevier (DOI): 10.1091/mbc.E10-06-0495

(DOI: 10.1091/mbc.E10-06-0495, PubMed: 20943950) Ayuko Sakane, Kazufumi Honda and Takuya Sasaki :
Rab13 regulates neurite outgrowth in PC12 cells through its effector protein, JRAB/MICAL-L2.,
Molecular and Cellular Biology, Vol.30, No.4, 1077-1087, 2010.

(要約): Neurite outgrowth is the first step in the processes of neuronal differentiation and regeneration and leads to synaptic polarization and plasticity. Rab13 small G protein shows an increased mRNA expression level during neuronal regeneration; it is therefore thought to be involved in this process. We previously identified JRAB (junctional Rab13-binding protein)/MICAL-L2 (molecules interacting with CasL-like 2) as a novel Rab13 effector protein. Here, we show that Rab13 regulates neurite outgrowth in the rat pheochromocytoma cell line PC12 through an interaction with JRAB/MICAL-L2. The expression of JRAB/MICAL-L2 alone inhibits neurite outgrowth, whereas coexpression of the dominant active form of Rab13 rescues this effect. We also demonstrate an intramolecular interaction between the N-terminal calponin-homology (CH) and LIM domains of JRAB/MICAL-L2 and the C-terminal coiled-coil domain. Finally, we show that the binding of Rab13 to JRAB/MICAL-L2 stimulates the interaction of JRAB/MICAL-L2 with actinin-4, an actin-binding protein, which localizes to the cell body and the tips of the neurites in PC12 cells. These results suggest that Rab13 and JRAB/MICAL-L2 may act to transfer actinin-4 from the cell body to the tips of neurites, where actinin-4 is involved in the reorganization of the actin cytoskeleton which results in neurite outgrowth.
(キーワード): Actins / Animals / Cytoskeletal Proteins / GTP Phosphohydrolases / Mice / Neurites / PC12 Cells / Protein Binding / Rats
(出版サイトへのリンク): ● Publication site (DOI): 10.1128/MCB.01067-09
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 20008558; ● Search Scopus @ Elsevier (PMID): 20008558; ● Search Scopus @ Elsevier (DOI): 10.1128/MCB.01067-09

(DOI: 10.1128/MCB.01067-09, PubMed: 20008558) Anita Szodorai, Yung-Hui Kuan, Silke Hunzelmann, Ulrike Engel, Ayuko Sakane, Takuya Sasaki, Yoshimi Takai, Joachim Kirsch, Ulrike Muller, Konrad Beyreuther, Scott Brady, Gerardo Morfini and Stefan Kins :
APP Anterograde Transport Requires Rab3A GTPase Activity for Assembly of the Transport Vesicle,
The Journal of Neuroscience, Vol.29, No.46, 14534-14544, 2009.

(要約): The amyloid precursor protein (APP) is anterogradely transported by conventional kinesin in a distinct transport vesicle, but both the biochemical composition of such a vesicle and the specific kinesin-1 motor responsible for transport are poorly defined. APP may be sequentially cleaved by beta- and gamma-secretases leading to accumulation of beta-amyloid (Abeta) peptides in brains of Alzheimer's disease patients, whereas cleavage of APP by alpha-secretases prevents Abeta generation. Here, we demonstrate by time-lapse analysis and immunoisolations that APP is a cargo of a vesicle containing the kinesin heavy chain isoform kinesin-1C, the small GTPase Rab3A, and a specific subset of presynaptic protein components. Moreover, we report that assembly of kinesin-1C and APP in this vesicle type requires Rab3A GTPase activity. Finally, we show cleavage of APP in transport vesicles by alpha-secretase activity, likely mediated by ADAM10. Together, these data indicate that maturation of APP transport vesicles, including recruitment of conventional kinesin, requires Rab3 GTPase activity.
(キーワード): Amyloid beta-Protein Precursor / Animals / Base Sequence / Cell Line, Tumor / Enzyme Activation / GTP Phosphohydrolases / Humans / Kinesin / Mice / Mice, Inbred C57BL / Mice, Knockout / Molecular Sequence Data / Protein Transport / Transport Vesicles / rab3A GTP-Binding Protein
(出版サイトへのリンク): ● Publication site (DOI): 10.1523/JNEUROSCI.1546-09.2009
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 19923287; ● Search Scopus @ Elsevier (PMID): 19923287; ● Search Scopus @ Elsevier (DOI): 10.1523/JNEUROSCI.1546-09.2009

(DOI: 10.1523/JNEUROSCI.1546-09.2009, PubMed: 19923287) Noriyuki Nishimura and Takuya Sasaki :
Rab family small G proteins in regulation of epithelial apical junctions.,
Frontiers in Bioscience, Vol.14, 2115-2129, 2009.

(要約): Tight junctions (TJs) and adherens junctions (AJs) comprise epithelial apical junctions that adhere neighboring epithelial cells and determine tissue organization. They are highly dynamic structures that undergo continuous remodeling during physiological morphogenesis and under pathological conditions. The assembly and disassembly of epithelial apical junctions is regulated by the interplay between a variety of cellular processes, such as the remodeling of actin cytoskeletons and the endocytic recycling of apical junctional proteins, and coordinated by many signaling pathways. Accumulating evidences demonstrate that Rab family small G proteins are crucially involved in the regulation of epithelial apical junctions. Rab proteins localized both at endosomes and apical junctions can influence the assembly and disassembly of epithelial apical junctions. In this review, we summarize how Rab proteins influence epithelial apical junctions and describe the role of Rab8/13-a junctional Rab13-binding protein (JRAB)/molecule interacting with CasL-like 2 (MICAL-L2) complexes in the regulation of epithelial apical junctions.
(キーワード): Endocytosis / Humans / Tight Junctions / rab GTP-Binding Proteins
(出版サイトへのリンク): ● Publication site (DOI): 10.2741/3366
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 19273188; ● Search Scopus @ Elsevier (PMID): 19273188; ● Search Scopus @ Elsevier (DOI): 10.2741/3366

(DOI: 10.2741/3366, PubMed: 19273188) Noriyuki Nishimura, Kunihiko Araki, Wakako Shinahara, Yumiko Nakano, Kaho Nishimura, Hironori Higashio and Takuya Sasaki :
Interaction of Rab3B with microtubule-binding protein Gas8 in NIH 3T3 cells.,
Archives of Biochemistry and Biophysics, Vol.474, No.1, 136-142, 2008.

(要約): Rab3 subfamily small G proteins (Rab3A, Rab3B, Rab3C, and Rab3D) control the regulated exocytosis in neuronal/secretory cells. Rab3B is also detected and upregulated in non-neuronal/non-secretory cells, whereas its function remains elusive. In the present study, we identified growth-arrest-specific gene 8 (Gas8), an evolutionally conserved microtubule-binding protein that is upregulated in growth-arrested NIH 3T3 cells and involved in the dynein motor regulation in flagellar/ciliary axoneme, as a novel Rab3B-binding protein using a yeast two-hybrid system. Rab3B as well as Gas8 was upregulated in growth-arrested NIH 3T3 cells and enriched in testis and lung with well-developed flagella/cilia. Gas8 was specifically interacted with the GTP-bound form of Rab3B and co-localized with Rab3B at the Golgi in NIH 3T3 cells. Furthermore, Rab3B was relocated upon expression of the Rab3B-binding domain of Gas8. These results suggest that Gas8 links Rab3B to microtubules in NIH 3T3 cells.
(キーワード): Animals / Blotting, Western / Cricetinae / Immunoprecipitation / Mice / Microscopy, Fluorescence / NIH 3T3 Cells / Protein Binding / Proteins / Reverse Transcriptase Polymerase Chain Reaction / Two-Hybrid System Techniques / rab3 GTP-Binding Proteins
(出版サイトへのリンク): ● Publication site (DOI): 10.1016/j.abb.2008.03.032
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 18396146; ● Search Scopus @ Elsevier (PMID): 18396146; ● Search Scopus @ Elsevier (DOI): 10.1016/j.abb.2008.03.032

(DOI: 10.1016/j.abb.2008.03.032, PubMed: 18396146) Hiroyoshi Nakatsuji, Noriyuki Nishimura, Rie Yamamura, Hiro-omi Kanayama and Takuya Sasaki :
Involvement of actinin-4 in the recruitment of JRAB/MICAL-L2 to cell-cell junctions and the formation of functional tight junctions.,
Molecular and Cellular Biology, Vol.28, No.10, 3324-3335, 2008.

(要約): Tight junctions (TJs) are cell-cell adhesive structures that undergo continuous remodeling. We previously demonstrated that Rab13 and a junctional Rab13-binding protein (JRAB)/molecule interacting with CasL-like 2 (MICAL-L2) localized at TJs and mediated the endocytic recycling of the integral TJ protein occludin and the formation of functional TJs. Here, we investigated how JRAB/MICAL-L2 was targeted to TJs. Using a series of deletion mutants, we found the plasma membrane (PM)-targeting domain within JRAB/MICAL-L2. We then identified actinin-4, which was originally isolated as an actin-binding protein associated with cell motility and cancer invasion/metastasis, as a binding protein for the PM-targeting domain of JRAB/MICAL-L2, using a yeast two-hybrid system. Actinin-4 was colocalized with JRAB/MICAL-L2 at cell-cell junctions and linked JRAB/MICAL-L2 to F-actin. Although actinin-4 bound to JRAB/MICAL-L2 without Rab13, the actinin-4-JRAB/MICAL-L2 interaction was enhanced by Rab13 activation. Depletion of actinin-4 by using small interfering RNA inhibited the recruitment of occludin to TJs during the Ca(2+) switch. During the epithelial polarization after replating, JRAB/MICAL-L2 was recruited from the cytosol to cell-cell junctions. This JRAB/MICAL-L2 recruitment as well as the formation of functional TJs was delayed in actinin-4-depleted cells. These results indicate that actinin-4 is involved in recruiting JRAB/MICAL-L2 to cell-cell junctions and forming functional TJs.
(キーワード): Actinin / Actins / Animals / Base Sequence / Binding Sites / Calcium / Cell Line / Cell Polarity / Cricetinae / Cytoskeletal Proteins / Epithelial Cells / Genetic Vectors / Intercellular Junctions / Membrane Proteins / Mice / Microfilament Proteins / Plasmids / Protein Binding / Protein Structure, Tertiary / RNA, Small Interfering / Recombinant Proteins / Sequence Deletion / Tight Junctions / Transfection / Two-Hybrid System Techniques / rab GTP-Binding Proteins
(出版サイトへのリンク): ● Publication site (DOI): 10.1128/MCB.00144-08
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 18332111; ● Search Scopus @ Elsevier (PMID): 18332111; ● Search Scopus @ Elsevier (DOI): 10.1128/MCB.00144-08

(DOI: 10.1128/MCB.00144-08, PubMed: 18332111) Hironori Higashio, Noriyuki Nishimura, Hiroyoshi Ishizaki, Jun Miyoshi, Satoshi Orita, Ayuko Sakane and Takuya Sasaki :
Doc2α and Munc13-4 Regulate Ca²⁺-Dependent Secretory Lysosome Exocytosis in Mast Cells.,
The Journal of Immunology, Vol.180, No.7, 4774-4784, 2008.

(要約): The Doc2 family comprises the brain-specific Doc2alpha and the ubiquitous Doc2beta and Doc2gamma. With the exception of Doc2gamma, these proteins exhibit Ca(2+)-dependent phospholipid-binding activity in their Ca(2+)-binding C2A domain and are thought to be important for Ca(2+)-dependent regulated exocytosis. In excitatory neurons, Doc2alpha interacts with Munc13-1, a member of the Munc13 family, through its N-terminal Munc13-1-interacting domain and the Doc2alpha-Munc13-1 system is implicated in Ca(2+)-dependent synaptic vesicle exocytosis. The Munc13 family comprises the brain-specific Munc13-1, Munc13-2, and Munc13-3, and the non-neuronal Munc13-4. We previously showed that Munc13-4 is involved in Ca(2+)-dependent secretory lysosome exocytosis in mast cells, but the involvement of Doc2 in this process is not determined. In the present study, we found that Doc2alpha but not Doc2beta was endogenously expressed in the RBL-2H3 mast cell line. Doc2alpha colocalized with Munc13-4 on secretory lysosomes, and interacted with Munc13-4 through its two regions, the N terminus containing the Munc13-1-interacting domain and the C terminus containing the Ca(2+)-binding C2B domain. In RBL-2H3 cells, Ca(2+)-dependent secretory lysosome exocytosis was inhibited by expression of the Doc2alpha mutant lacking either of the Munc13-4-binding regions and the inhibition was suppressed by coexpression of Munc13-4. Knockdown of endogenous Doc2alpha also reduced Ca(2+)-dependent secretory lysosome exocytosis, which was rescued by re-expression of human Doc2alpha but not by its mutant that could not bind to Munc13-4. Moreover, Ca(2+)-dependent secretory lysosome exocytosis was severely reduced in bone marrow-derived mast cells from Doc2alpha knockout mice. These results suggest that the Doc2alpha-Muunc13-4 system regulates Ca(2+)-dependent secretory lysosome exocytosis in mast cells.
(キーワード): Animals / Antigens / Bone Marrow / カルシウム (calcium) / Calcium-Binding Proteins / Cell Line / Cercopithecus aethiops / Exocytosis / Gene Expression Regulation / Humans / Ionophores / Lysosomes / Mast Cells / Membrane Proteins / Mice / Nerve Tissue Proteins / Phorbol Esters / Protein Binding / Rats
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 18354201; ● Search Scopus @ Elsevier (PMID): 18354201

(PubMed: 18354201) I. Kanda, Noriyuki Nishimura, H. Nakatsuji, R. Yamamura, Hideki Nakanishi and Takuya Sasaki :
Involvement of Rab13 and JRAB/MICAL-L2 in epithelial cell scattering.,
Oncogene, Vol.27, No.12, 1687-1695, 2008.

(要約): Epithelial cell scattering recapitulates the first steps of carcinoma invasion/metastasis. While the balance between cell-cell adhesive activity and cell motility ultimately determines this process, its molecular mechanisms remain unclear. Adherence junctions and tight junctions (TJs) are primarily responsible for cell-cell adhesive activity and subjected to dynamic remodeling. We previously showed that Rab13 and its effector protein JRAB/MICAL-L2 mediate the endocytic recycling of the integral TJ protein occludin and the assembly of functional TJs. In this study, we examined the role of Rab13 and JRAB/MICAL-L2 in the scattering of Madin-Darby canine kidney (MDCK) cells in response to 12-O-tetradecanoylphorbol-13-acetate (TPA). Knockdown of Rab13 in canine MDCK cells suppressed the TPA-induced scattering, and this phenotype was restored by re-expression of human Rab13. During TPA-induced MDCK cell scattering, Rab13 was transiently activated and returned to its basal level, and both Rab13 and JRAB/MICAL-L2 were colocalized with F-actin at cell-cell contact sites and then accumulated at emerging lamellipodial structures. TPA-induced MDCK cell scattering was also inhibited by knockdown of canine JRAB/MICAL-L2 and rescued by re-expression of mouse JRAB/MICAL-L2. These results indicate that Rab13 and JRAB/MICAL-L2 are involved in epithelial cell scattering.
(キーワード): Animals / Carcinogens / Cell Adhesion / Cell Line / Cell Movement / Cricetinae / Cytoskeletal Proteins / Dogs / Epithelial Cells / Humans / Microfilament Proteins / Tetradecanoylphorbol Acetate / rab GTP-Binding Proteins
(出版サイトへのリンク): ● Publication site (DOI): 10.1038/sj.onc.1210812
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 17891173; ● Search Scopus @ Elsevier (PMID): 17891173; ● Search Scopus @ Elsevier (DOI): 10.1038/sj.onc.1210812

(DOI: 10.1038/sj.onc.1210812, PubMed: 17891173) Rie Yamamura, Noriyuki Nishimura, Hiroyoshi Nakatsuji, Seiji Arase and Takuya Sasaki :
The Interaction of JRAB/MICAL-L2 with Rab8 and Rab13 Coordinates the Assembly of Tight Junctions and Adherens Junctions.,
Molecular Biology of the Cell, Vol.19, No.3, 971-983, 2008.

(要約): The assembly of tight junctions (TJs) and adherens junctions (AJs) is regulated by the transport of integral TJ and AJ proteins to and/or from the plasma membrane (PM) and it is tightly coordinated in epithelial cells. We previously reported that Rab13 and a junctional Rab13-binding protein (JRAB)/molecule interacting with CasL-like 2 (MICAL-L2) mediated the endocytic recycling of an integral TJ protein occludin and the formation of functional TJs. Here, we investigated the role of Rab13 and JRAB/MICAL-L2 in the transport of other integral TJ and AJ proteins claudin-1 and E-cadherin to the PM by using a Ca(2+)-switch model. Although knockdown of Rab13 specifically suppressed claudin-1 and occludin but not E-cadherin transport, knockdown of JRAB/MICAL-L2 and expression of its Rab13-binding domain (JRAB/MICAL-L2-C) inhibited claudin-1, occludin, and E-cadherin transport. We then identified Rab8 as another JRAB/MICAL-L2-C-binding protein. Knockdown of Rab8 inhibited the Rab13-independent transport of E-cadherin to the PM. Rab8 and Rab13 competed with each other for the binding to JRAB/MICAL-L2 and functionally associated with JRAB/MICAL-L2 at the perinuclear recycling/storage compartments and PM, respectively. These results suggest that the interaction of JRAB/MICAL-L2 with Rab8 and Rab13 coordinates the assembly of AJs and TJs.
(キーワード): Adherens Junctions / Animals / Binding, Competitive / Cadherins / Cell Line / Cytoskeletal Proteins / Endocytosis / Humans / Intracellular Space / Membrane Proteins / Models, Biological / Protein Binding / Protein Structure, Tertiary / Protein Transport / Tight Junctions / rab GTP-Binding Proteins
(出版サイトへのリンク): ● Publication site (DOI): 10.1091/mbc.E07-06-0551
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 18094055; ● Search Scopus @ Elsevier (PMID): 18094055; ● Search Scopus @ Elsevier (DOI): 10.1091/mbc.E07-06-0551

(DOI: 10.1091/mbc.E07-06-0551, PubMed: 18094055) Ayuko Sakane, Miyoshi Jun, Takai Yoshimi and Takuya Sasaki :
Analysis on the Emerging Role of Rab3 GTPase-Activating Protein in Warburg Micro and Martsolf Syndrome.,
Methods in Enzymology, Vol.438, 131-139, 2008.

(要約): Evidence is accumulating that Rab3A plays a key role in neurotransmitter release and synaptic plasticity. Recently mutations in the catalytic subunit p130 and the noncatalytic subunit p150 of Rab3 GTPase-activating protein were found to cause Warburg Micro syndrome and Martsolf syndrome, respectively, both of which exhibit mental retardation. We have found that loss of p130 in mice results in inhibition of Ca2+-dependent glutamate release from cerebrocortical synaptosomes and alters short-term plasticity in the hippocampal CA1 region, probably through the accumulation of the GTP-bound form of Rab3A. Here, we describe the procedures for the measurement of the GTP-bound pool of Rab3A with pull-down assay using mouse brains and the biochemical method for the measurement of glutamate release from mouse synaptosomes.
(キーワード): Abnormalities, Multiple / Animals / Calcium / Cricetinae / Glutamic Acid / Humans / Mice / Synaptosomes / Syndrome / rab3 GTP-Binding Proteins / rab3A GTP-Binding Protein
(出版サイトへのリンク): ● Publication site (DOI): 10.1016/S0076-6879(07)38009-9
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 18413245; ● Summary page in Scopus @ Elsevier: 2-s2.0-45549089488

(DOI: 10.1016/S0076-6879(07)38009-9, PubMed: 18413245, Elsevier: Scopus) Noriyuki Nishimura and Takuya Sasaki :
Identification and Characterization of JRAB/MICAL-L2, a Junctional Rab13-Binding Protein.,
Methods in Enzymology, Vol.438, 141-153, 2008.

(要約): The Rab family small G proteins are localized to distinct subsets of intracellular membranes and play a key role in membrane traffic through the interaction with their specific effector protein(s). Rab13 is identified as a plaque protein at tight junctions (TJs) and has been shown to regulate the assembly of functional TJs in epithelial cells. We have demonstrated that Rab13 mediates the endocytic recycling of integral TJ protein occludin, and identified a junctional Rab13-binding protein (JRAB)/molecule interacting with CasL-like 2 (MICAL-L2) as a Rab13 effector protein using a yeast two-hybrid system. JRAB/MICAL-L2 has a calponin-homology domain in the N-terminus, a LIM domain in the middle, and a coiled-coil domain at the C-terminus, and specifically binds to the GTP-bound form of Rab13 via its C-terminus. It is localized to TJs in epithelial cells and distributed along stress fibers in fibroblasts. In epithelial cells, JRAB/MICAL-L2 as well as Rab13 mediates the endocytic recycling of occludin, but not transferrin receptor, and the formation of functional TJs. This chapter describes the procedures for the isolation of JRAB/MICAL-L2 and the analysis of its functions.
(キーワード): Animals / Cricetinae / Humans / Mice / Microfilament Proteins / NIH 3T3 Cells / Tight Junctions / Two-Hybrid System Techniques
(出版サイトへのリンク): ● Publication site (DOI): 10.1016/S0076-6879(07)38010-5
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 18413246; ● Search Scopus @ Elsevier (PMID): 18413246; ● Search Scopus @ Elsevier (DOI): 10.1016/S0076-6879(07)38010-5

(DOI: 10.1016/S0076-6879(07)38010-5, PubMed: 18413246) Noriyuki Nishimura and Takuya Sasaki :
Regulation of epithelial cell adhesion and repulsion : role of endocytic recycling.,
The Journal of Medical Investigation : JMI, Vol.55, No.1-2, 9-16, 2008.

(要約): A proper balance between cell adhesion and repulsion is essential for cellular morphogenesis during epithelial-mesenchymal transition and mesenchymal-epithelial transition. A number of ligand-receptor pairs including hepatocyte growth factor/scatter factor-Met and semaphorin-plexin are known to control this balance through the complex intracellular signaling pathways. Cell adhesion to other cells and extracellular matrix (ECM) is mediated by cell adhesion molecules (CAMs) and ECM receptors, respectively, which are associated with cytoskeleton through a variety of plaque proteins strengthening and/or weakening adhesion activities. Cell repulsion requires the downregulation of cell adhesion and the extensive changes in cytoskeletal dynamics. The endocytic recycling of CAMs and ECM receptors has recently emerged as an important mechanism to control the balance between cell adhesion and repulsion. Molecule interacting with CasL (MICAL) family proteins are originally identified as a plaque protein associated with ECM receptors integrins and implicated in semaphorin-plexin dependent repulsive axon guidance. We have recently shown that MICAL family protein JRAB/MICAL-L2 functions as an effector protein for Rab family small G protein Rab13 and regulates the endocytic recycling of tight junctional CAM occludin and controls the adhesion and repulsion of epithelial cells.
(キーワード): Animals / Cell Adhesion / Cell Adhesion Molecules / Cytoskeletal Proteins / Cytoskeleton / Endocytosis / Epithelial Cells / Extracellular Matrix / Humans / Signal Transduction / rab GTP-Binding Proteins
(徳島大学機関リポジトリ): ● Metadata: 110833
(出版サイトへのリンク): ● Publication site (DOI): 10.2152/jmi.55.9
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 18319540; ● Search Scopus @ Elsevier (PMID): 18319540; ● Search Scopus @ Elsevier (DOI): 10.2152/jmi.55.9

(徳島大学機関リポジトリ: 110833, DOI: 10.2152/jmi.55.9, PubMed: 18319540) Noriyuki Nishimura and Takuya Sasaki :
Cell-Surface Biotinylation to Study Endocytosis and Recycling of Occludin.,
Methods in Molecular Biology, Vol.440, 89-96, 2008.

(要約): The dynamic turnover of adherens junctions (AJs) and tight junctions (TJs) is essential for epithelial morphogenesis during normal development and differentiation. Although the endocytic recycling of E-cadherin is characterized and implicated in AJ turnover, the molecular basis for TJ turnover is poorly understood. Occludin and claudins are distinct transmembrane proteins localized to the TJs. Although claudins are an indispensable structural component of TJ strands, depletion of occludin in mice reveals well-developed TJ strands and complex histological abnormalities. To examine the intracellular transport of transmembrane proteins to and from the cell surface, cell-surface biotinylation is a proven powerful method. Using this method, we successfully demonstrated that occludin was endocytosed and recycled back to the cell surface in both fibroblastic baby hamster kidney (BHK) and epithelial MTD-1A cells. The endocytic recycling of occludin as well as the formation of functional TJs was dependent on Rab13 and a junctional Rab13-binding protein (JRAB)/molecule interacting with CasL-like 2 (MICAL-L2). We describe the method to study the intracellular transport of occludin to and from the cell surface in both fibroblastic and epithelial cells.
(キーワード): Animals / Biological Assay / Biotinylation / Cell Line / Cell Line, Tumor / Cell Membrane / Cricetinae / Cytoskeletal Proteins / Endocytosis / Epithelial Cells / Fibroblasts / Humans / Membrane Proteins / Mice / Recombinant Proteins / Tight Junctions / rab GTP-Binding Proteins
(出版サイトへのリンク): ● Publication site (DOI): 10.1007/978-1-59745-178-9_7
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 18369939; ● Search Scopus @ Elsevier (PMID): 18369939; ● Search Scopus @ Elsevier (DOI): 10.1007/978-1-59745-178-9_7

(DOI: 10.1007/978-1-59745-178-9_7, PubMed: 18369939) Ayuko Sakane, Shigetsugu Hatakeyama and Takuya Sasaki :
Involvement of Rabring7 in EGF receptor degradation as an E3 ligase.,
Biochemical and Biophysical Research Communications, Vol.357, No.4, 1058-1064, 2007.

(要約): Rab7, a member of the Rab family small G proteins, is involved in the late stage of the endocytic pathway. We previously identified a Rab7 target protein, Rabring7, which contains a RING finger domain at its C termini, but the precise role of Rabring7 remains unknown. In this study, we demonstrate using an in vitro ubiquitination assay with recombinant E1 and E2 proteins that Rabring7 has E3 ligase activity and that it preferentially reacts with Ubc4 and Ubc5 as its E2 proteins. Rabring7 ubiquitinated itself but not Rab7, and a mutation at Cys-229 in the RING finger domain (Rabring7C229S) completely diminished its E3 ligase activity. In the ligand-induced degradation of EGF receptor (EGFR), Rabring7 accelerated the degradation of EGFR, whereas Rabring7C229S inhibited the degradation induced by cCbl, another E3 ligase. These results suggest that Rabring7 is involved in the endocytic trafficking of EGFR through its E3 ligase activity.
(キーワード): Cell Line / Endocytosis / Enzyme Activation / Humans / Intracellular Signaling Peptides and Proteins / Kidney / Protein Binding / Receptor, Epidermal Growth Factor / Ubiquitin-Protein Ligases
(出版サイトへのリンク): ● Publication site (DOI): 10.1016/j.bbrc.2007.04.052
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 17462600; ● Search Scopus @ Elsevier (PMID): 17462600; ● Search Scopus @ Elsevier (DOI): 10.1016/j.bbrc.2007.04.052

(DOI: 10.1016/j.bbrc.2007.04.052, PubMed: 17462600) Ayuko Sakane, Shinji Manabe, Hiroyoshi Ishizaki, Miki Tanaka-Okamoto, Emi Kiyokage, Kazunori Toida, Takayuki Yoshida, Jun Miyoshi, Haruyuki Kamiya, Yoshimi Takai and Takuya Sasaki :
Rab3 GTPase-activating protein regulates synaptic transmission and plasticity through the inactivation of Rab3.,
Proceedings of the National Academy of Sciences of the United States of America, Vol.103, No.26, 10029-10034, 2006.

(要約): Rab3A small G protein is a member of the Rab family and is most abundant in the brain, where it is localized on synaptic vesicles. Evidence is accumulating that Rab3A plays a key role in neurotransmitter release and synaptic plasticity. Rab3A cycles between the GDP-bound inactive and GTP-bound active forms, and this change in activity is associated with the trafficking cycle of synaptic vesicles at nerve terminals. Rab3 GTPase-activating protein (GAP) stimulates the GTPase activity of Rab3A and is expected to determine the timing of the dissociation of Rab3A from synaptic vesicles, which may be coupled with synaptic vesicle exocytosis. Rab3 GAP consists of two subunits: the catalytic subunit p130 and the noncatalytic subunit p150. Recently, mutations in p130 were found to cause Warburg Micro syndrome with severe mental retardation. Here, we generated p130-deficient mice and found that the GTP-bound form of Rab3A accumulated in the brain. Loss of p130 in mice resulted in inhibition of Ca(2+)-dependent glutamate release from cerebrocortical synaptosomes and altered short-term plasticity in the hippocampal CA1 region. Thus, Rab3 GAP regulates synaptic transmission and plasticity by limiting the amount of the GTP-bound form of Rab3A.
(キーワード): Animals / Calcium / Glutamic Acid / Hippocampus / Mice / Mice, Mutant Strains / Neuronal Plasticity / Synapses / Synaptic Transmission / Synaptosomes / rab3 GTP-Binding Proteins / rab3A GTP-Binding Protein
(出版サイトへのリンク): ● Publication site (DOI): 10.1073/pnas.0600304103
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 16782817; ● Search Scopus @ Elsevier (PMID): 16782817; ● Search Scopus @ Elsevier (DOI): 10.1073/pnas.0600304103

(DOI: 10.1073/pnas.0600304103, PubMed: 16782817) Tomoya Terai, Noriyuki Nishimura, Ikuno Kanda, Natsuo Yasui and Takuya Sasaki :
JRAB/MICAL-L2 is a junctional Rab13-binding protein mediating the endocytic recycling of occludin.,
Molecular Biology of the Cell, Vol.17, No.5, 2465-2475, 2006.

(要約): The dynamic turnover of tight junctions (TJs) is essential for epithelial-mesenchymal transitions and/or mesenchymal-epithelial transitions during epithelial morphogenesis. We previously demonstrated that Rab13 specifically mediates the endocytic recycling of occludin. Here, we identified MICAL-L2 (molecule interacting with CasL-like 2) as a novel Rab13-binding protein. Immunoprecipitation and immunofluorescence microscopy showed that MICAL-L2 specifically bound to the GTP-bound form of Rab13 via its C terminus, which contained a coiled-coil domain, and localized at TJs in epithelial MTD-1A cells. Recycling assay demonstrated that a MICAL-L2 mutant lacking the Rab13-binding domain (MICAL-L2-N) specifically inhibited the endocytic recycling of occludin but not transferrin receptor. Ca2+ switch assay further revealed that MICAL-L2-N as well as Rab13 Q67L inhibited the recruitment of occludin to the plasma membrane, the development of transepithelial electrical resistance, and the formation of a paracellular diffusion barrier. MICAL-L2 was displaced from TJs upon actin depolymerization and was distributed along radiating actin cables and stress fibers in Ca2+-depleted MTD-1A and fibroblastic NIH3T3 cells, respectively. These results suggest that MICAL-L2 mediates the endocytic recycling of occludin and the formation of functional TJs by linking Rab13 to actin cytoskeleton. We rename MICAL-L2 as JRAB (junctional Rab13-binding protein).
(キーワード): Actin Cytoskeleton / Amino Acid Sequence / Animals / Calcium / Cytoskeletal Proteins / Dogs / Endocytosis / Epithelium / Fibroblasts / Membrane Proteins / Mice / Molecular Sequence Data / Mutation / NIH 3T3 Cells / Protein Structure, Tertiary / Tight Junctions / rab GTP-Binding Proteins
(出版サイトへのリンク): ● Publication site (DOI): 10.1091/mbc.E05-09-0826
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 16525024; ● Search Scopus @ Elsevier (PMID): 16525024; ● Search Scopus @ Elsevier (DOI): 10.1091/mbc.E05-09-0826

(DOI: 10.1091/mbc.E05-09-0826, PubMed: 16525024) Kouichi Mizuno, Ayuko Sakane and Takuya Sasaki :
Rabring7: A target protein for Rab7 small G protein.,
Methods in Enzymology, Vol.403, 687-696, 2005.

(要約): Rab7, a member of the Rab family of small G proteins, has been shown to regulate late endocytic traffic and lysosome biogenesis, but the exact roles and the mode of actions of Rab7 are still undetermined. Accumulating evidence suggests that each Rab protein has multiple target proteins and works together with them to coordinate the individual step of vesicle traffic. Rabring7 (Rab7-interacting ring finger protein) is a Rab7 target protein that has been isolated using a CytoTrap system. This protein shows no homology with RILP, which has been reported as another Rab7 target protein. Rabring7 is recruited efficiently to late endosome/lysosome by the GTP-bound form of Rab7. Exogenous expression of Rabring7 not only affects epidermal growth factor degradation but also induces the perinuclear aggregation of lysosomes and the increased acidity in the lysosomes. This chapter describes the procedures for the isolation of Rabring7 with a CytoTrap system, the analysis of the Rab7-Rabring7 interactions, and the properties of Rabring7.
(キーワード): Animals / Cell Line / Cricetinae / Green Fluorescent Proteins / Humans / Immunoprecipitation / Protein Binding / rab GTP-Binding Proteins
(出版サイトへのリンク): ● Publication site (DOI): 10.1016/S0076-6879(05)03059-4
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 16473630; ● Search Scopus @ Elsevier (PMID): 16473630; ● Search Scopus @ Elsevier (DOI): 10.1016/S0076-6879(05)03059-4

(DOI: 10.1016/S0076-6879(05)03059-4, PubMed: 16473630) Shinya Morimoto, Noriyuki Nishimura, Tomoya Terai, Shinji Manabe, Yasuyo Yamamoto, Wakako Shinahara, Hidenori Miyake, Seiki Tashiro, Mitsuo Shimada and Takuya Sasaki :
Rab13 Mediates the Continuous Endocytic Recycling of Occludin to the Cell Surface,
The Journal of Biological Chemistry, Vol.280, No.3, 2220-2228, 2005.

(要約): During epithelial morphogenesis, adherens junctions (AJs) and tight junctions (TJs) undergo dynamic reorganization, whereas epithelial polarity is transiently lost and reestablished. Although ARF6-mediated endocytic recycling of E-cadherin has been characterized and implicated in the rapid remodeling of AJs, the molecular basis for the dynamic rearrangement of TJs remains elusive. Occludin and claudins are integral membrane proteins comprising TJ strands and are thought to be responsible for establishing and maintaining epithelial polarity. Here we investigated the intracellular transport of occludin and claudins to and from the cell surface. Using cell surface biotinylation and immunofluorescence, we found that a pool of occludin was continuously endocytosed and recycled back to the cell surface in both fibroblastic baby hamster kidney cells and epithelial MTD-1A cells. Biochemical endocytosis and recycling assays revealed that a Rab13 dominant active mutant (Rab13 Q67L) inhibited the postendocytic recycling of occludin, but not that of transferrin receptor and polymeric immunoglobulin receptor in MTD-1A cells. Double immunolabelings showed that a fraction of endocytosed occludin was colocalized with Rab13 in MTD-1A cells. These results suggest that Rab13 specifically mediates the continuous endocytic recycling of occludin to the cell surface in both fibroblastic and epithelial cells.
(キーワード): Adherens Junctions / Animals / Biotin / Cadherins / Cell Line / Endocytosis / Humans / Membrane Proteins / Microscopy, Fluorescence / Tight Junctions / rab GTP-Binding Proteins
(出版サイトへのリンク): ● Publication site (DOI): 10.1074/jbc.M406906200
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 15528189; ● Search Scopus @ Elsevier (PMID): 15528189; ● Search Scopus @ Elsevier (DOI): 10.1074/jbc.M406906200

(DOI: 10.1074/jbc.M406906200, PubMed: 15528189) Keiichi Goishi, Kouichi Mizuno, Hideki Nakanishi and Takuya Sasaki :
Involvement of Rab27 in antigen-induced histamine release from rat basophilic leukemia 2H3 cells,
Biochemical and Biophysical Research Communications, Vol.324, No.1, 294-301, 2004.

(要約): The Rab family small G proteins regulate discrete steps in vesicular transport pathways. Recent studies indicate that one member of the Rab family, Rab27A, regulates the transport of lysosome-related organelles, such as melanosome distribution in melanocytes, lytic granule release in cytotoxic T cells, and dense granule release in platelets. Here, we have examined the involvement of Rab27A in the exocytic transport of another lysosome-related organelle, the basophilic secretory granule, in basophils. We have found that Rab27A locates on basophilic secretory granules containing histamine in rat basophilic leukemia (RBL) 2H3 cells. In addition, exogenous expression of dominant active Rab27A reduces antigen-induced histamine release from the cells. We have moreover identified Munc13-4 as a Rab27A target using a CytoTrap system and found that exogenous expression of Munc13-4 affects antigen-induced histamine release from RBL-2H3 cells. These results demonstrate that Rab27A plays a crucial role in antigen-induced histamine release from RBL-2H3 cells.
(キーワード): Rab27A / Histamine release / Basophil / Lentiviral vector / Munc13-4
(出版サイトへのリンク): ● Publication site (DOI): 10.1016/j.bbrc.2004.09.050
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 15465017; ● Search Scopus @ Elsevier (PMID): 15465017; ● Search Scopus @ Elsevier (DOI): 10.1016/j.bbrc.2004.09.050

(DOI: 10.1016/j.bbrc.2004.09.050, PubMed: 15465017) Shinji Manabe, Noriyuki Nishimura, Yasuyo Yamamoto, Hiroko Kitamura, Shinya Morimoto, Mayu Imai, Shinji Nagahiro, Susumu Seino and Takuya Sasaki :
Identification and characterization of Noc2 as a potential Rab3B effector protein in epithelial cells,
Biochemical and Biophysical Research Communications, Vol.316, No.1, 218-225, 2004.

(要約): The Rab3 family small G proteins (Rab3A-D) are involved in the regulated secretory pathway of brain and secretory tissues. Among Rab3-interacting proteins, Rabphilin-3, Rim, and Noc2, all of which contain a conserved Rab3-binding domain (RBD3), are generally recognized Rab3 effector proteins in neurons and secretory cells. Although Rab3B was also detected in epithelial cells, its function remained unknown. We isolated cDNA sequences from human epithelial Caco2-cell mRNA by degenerate RT-PCR based on the conserved amino acid sequence of RBD3. Multiple cDNA clones were identified as encoding Noc2. Northern blot analysis revealed that Noc2 mRNA was expressed not only in secretory tissues but also in epithelial tissues and cell lines. A pull-down assay demonstrated that Noc2 bound to Rab3B in a GTP-dependent manner. When Noc2 was co-expressed with the GTP-bound form of Rab3B, it was recruited from the cytosol to perinuclear membranes. Furthermore, overexpression of Noc2 inhibited the cell-surface transport of basolateral vesicular stomatitis virus glycoprotein. These results suggest that Noc2 functions as a potential Rab3B effector protein in epithelial cells.
(キーワード): Author Keywords / Rab / Epithelial cells / RBD3 / Noc2 / VSV-G
(出版サイトへのリンク): ● Publication site (DOI): 10.1016/j.bbrc.2004.02.026
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 15003533; ● Search Scopus @ Elsevier (PMID): 15003533; ● Search Scopus @ Elsevier (DOI): 10.1016/j.bbrc.2004.02.026

(DOI: 10.1016/j.bbrc.2004.02.026, PubMed: 15003533) Hirokazu Nakahara, Tomohiro Otani, Takuya Sasaki, Yasuhiro Miura, Yoshimi Takai and Mikihiko Kogo :
Involvement of Cdc42 and Rac small G proteins in invadopodia formation of RPMI7951 cells.,
Genes to Cells, Vol.8, No.12, 1019-1027, 2003.

(要約): Invadopodia are membrane protrusions into the extracellular matrix by aggressive tumour cells. These structures are associated with sites of matrix degradation and invasiveness of malignant tumour cells in an in vitro fibronectin degradation/invasion assay. The Rho family small G proteins, consisting of the Rho, Rac and Cdc42 subfamilies, are implicated in various cell functions, such as cell shape change, adhesion, and motility, through reorganization of the actin cytoskeleton. We studied the roles of the Rho family small G proteins in invadopodia formation. We first demonstrated that invadopodia of RPMI7951 human melanoma cells extended into the matrix substratum on a vertical view using a laser scanning confocal microscope system. We confirmed that invadopodia were rich in actin filaments (F-actin) and visualized clearly with F-actin staining on a vertical view as well as on a horizontal view. We then studied the roles of Rho, Rac, and Cdc42 in invasiveness of the same cell line. In the in vitro fibronectin degradation/invasion assay, a dominant active mutant of Cdc42 enhanced dot-like degradation, whereas a dominant active mutant of Rac enhanced diffuse-type degradation. Furthermore, frabin, a GDP/GTP exchange protein for Cdc42 with F-actin-binding activity, enhanced both dot-like and diffuse-type degradation. However, a dominant active mutant of Rho did not affect the fibronectin degradation. Moreover, inhibition of phosphatidylinositol-3 kinase (PI3K) disrupted the Rac and Cdc42-dependent actin structures and blocked the fibronectin degradation. These results suggest that Cdc42 and Rac play important roles in fibronectin degradation and invasiveness in a coordinate manner through the frabin-Cdc42/Rac-PI3K signalling pathway.
(キーワード): Actins / Cell Line, Tumor / Cell Membrane Structures / Cell Size / Fibronectins / Guanine Nucleotide Exchange Factors / Humans / Melanoma / Neoplasm Invasiveness / Phosphatidylinositol 3-Kinases / cdc42 GTP-Binding Protein / rac GTP-Binding Proteins
(出版サイトへのリンク): ● Publication site (DOI): 10.1111/j.1365-2443.2003.00695.x
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 14750956; ● Search Scopus @ Elsevier (PMID): 14750956; ● Search Scopus @ Elsevier (DOI): 10.1111/j.1365-2443.2003.00695.x

(DOI: 10.1111/j.1365-2443.2003.00695.x, PubMed: 14750956) Kouichi Mizuno, Akiko Kitamura and Takuya Sasaki :
Rabring7, a novel Rab7 target protein with a RING finger motif,
Molecular Biology of the Cell, Vol.14, No.9, 3741-3752, 2003.

(要約): Rab7, a member of the Rab family small G proteins, has been shown to regulate intracellular vesicle traffic to late endosome/lysosome and lysosome biogenesis, but the exact roles of Rab7 are still undetermined. Accumulating evidence suggests that each Rab protein has multiple target proteins that function in the exocytic/endocytic pathway. We have isolated a new Rab7 target protein, Rabring7 (Rab7-interacting RING finger protein), using a CytoTrap system. It contains an H2 type RING finger motif at the C termini. Rabring7 shows no homology with RILP, which has been reported as another Rab7 target protein. GST pull-down and coimmunoprecipitation assays demonstrate that Rabring7 specifically binds the GTP-bound form of Rab7 at the N-terminal portion. Rabring7 is found mainly in the cytosol and is recruited efficiently to late endosomes/lysosomes by the GTP-bound form of Rab7 in BHK cells. Overexpression of Rabring7 not only affects epidermal growth factor degradation but also causes the perinuclear aggregation of lysosomes, in which the accumulation of the acidotropic probe LysoTracker is remarkably enhanced. These results suggest that Rabring7 plays crucial roles as a Rab7 target protein in vesicle traffic to late endosome/lysosome and lysosome biogenesis.
(キーワード): Adaptor Proteins, Signal Transducing / Amino Acid Motifs / Amino Acid Sequence / Animals / COS Cells / Carrier Proteins / Cells, Cultured / Cercopithecus aethiops / Endocytosis / Epidermal Growth Factor / Exocytosis / Gene Library / Humans / Intracellular Signaling Peptides and Proteins / Lysosomes / Mice / Molecular Sequence Data / Mutation / Protein Transport / rab GTP-Binding Proteins
(出版サイトへのリンク): ● Publication site (DOI): 10.1091/mbc.E02-08-0495
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 12972561; ● Search Scopus @ Elsevier (PMID): 12972561; ● Search Scopus @ Elsevier (DOI): 10.1091/mbc.E02-08-0495

(DOI: 10.1091/mbc.E02-08-0495, PubMed: 12972561) Yasuyo Yamamoto, Noriyuki Nishimura, Shinya Morimoto, Hiroko Kitamura, Shinji Manabe, Hiro-omi Kanayama, Susumu Kagawa and Takuya Sasaki :
Distinct roles of Rab3B and Rab13 in the polarized transport of apical, basolateral, and tight junctional membrane proteins to the plasma membrane,
Biochemical and Biophysical Research Communications, Vol.308, No.2, 270-275, 2003.

(要約): Regulated transport of proteins to distinct plasma membrane domains is essential for the establishment and maintenance of cell polarity in all eukaryotic cells. The Rab family small G proteins play a crucial role in determining the specificity of vesicular transport pathways. Rab3B and Rab13 localize to tight junction in polarized epithelial cells and cytoplasmic vesicular structures in non-polarized fibroblasts, but their functions are poorly understood. Here we examined their roles in regulating the cell-surface transport of apical p75 neurotrophin receptor (p75NTR), basolateral low-density lipoprotein receptor (LDLR), and tight junctional Claudin-1 using transport assay in non-polarized fibroblasts. Overexpression of Rab3B mutants inhibited the cell-surface transport of LDLR, but not p75NTR and Claudin-1. In contrast, overexpression of Rab13 mutants impaired the transport of Claudin-1, but not LDLR and p75NTR. These results suggest that Rab3B and Rab13 direct the cell-surface transport of LDLR and Claudin-1, respectively, and may contribute to epithelial polarization.
(キーワード): Rab3B / Rab13 / Polarized transport / Tight junction / Claudins
(出版サイトへのリンク): ● Publication site (DOI): 10.1016/S0006-291X(03)01358-5
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 12901864; ● Search Scopus @ Elsevier (PMID): 12901864; ● Search Scopus @ Elsevier (DOI): 10.1016/S0006-291X(03)01358-5

(DOI: 10.1016/S0006-291X(03)01358-5, PubMed: 12901864) F Nagano, H Kawabe, H Nakanishi, M Shimohara, M Eeguchi-Tewarada, M Takeuchi, Takuya Sasaki and Y Takai :
Rabconnection-3: A novel protein that binds GDP/GTP exchange protein and GTPase-activating protein for Rab3 small G protein family,
The Journal of Biological Chemistry, Vol.277, No.12, 9629-9632, 2002.

(要約): Rab3A, a member of the Rab3 small G protein family, regulates Ca(2+)-dependent exocytosis of neurotransmitter. The cyclical activation and inactivation of Rab3A are essential for the Rab3A action in exocytosis. GDP-Rab3A is activated to GTP-Rab3A by Rab3 GDP/GTP exchange protein (Rab3 GEP), and GTP-Rab3A is inactivated to GDP-Rab3A by Rab3 GTPase-activating protein (Rab3 GAP). It remains unknown how or in which step of the multiple exocytosis steps these regulators are activated and inactivated. We isolated here a novel protein that was co-immunoprecipitated with Rab3 GEP and GAP by their respective antibodies from the crude synaptic vesicle fraction of rat brain. The protein, named rabconnectin-3, bound both Rab3 GEP and GAP. The cDNA of rabconnectin-3 was cloned from a human cDNA library and its primary structure was determined. Human rabconnectin-3 consisted of 3,036 amino acids and showed a calculated M(r) of 339,753. It had 12 WD domains. Tissue and subcellular distribution analyses in rat indicated that rabconnectin-3 was abundantly expressed in the brain where it was enriched in the synaptic vesicle fraction. Immunofluorescence and immunoelectron microscopy revealed that rabconnectin-3 was concentrated on synaptic vesicles at synapses. These results indicate that rabconnectin-3 serves as a scaffold molecule for both Rab3 GEP and GAP on synaptic vesicles.
(キーワード): Adaptor Proteins, Signal Transducing / Amino Acid Sequence / Animals / Brain / Calcium / Carrier Proteins / Cloning, Molecular / Connectin / DNA, Complementary / Electrophoresis, Polyacrylamide Gel / Exocytosis / GTPase-Activating Proteins / Glutathione Transferase / Humans / Microscopy, Fluorescence / Microscopy, Immunoelectron / Molecular Sequence Data / Muscle Proteins / Nerve Tissue Proteins / Precipitin Tests / Protein Binding / Protein Kinases / Protein Structure, Tertiary / Rats / Recombinant Fusion Proteins / Subcellular Fractions / Tissue Distribution / rab3 GTP-Binding Proteins
(出版サイトへのリンク): ● Publication site (DOI): 10.1074/jbc.C100730200
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 11809763; ● Summary page in Scopus @ Elsevier: 2-s2.0-0037155930

(DOI: 10.1074/jbc.C100730200, PubMed: 11809763, Elsevier: Scopus) H. Nakanishi, Takuya Sasaki and Y. Takai :
Isolation of regulator proteins for the Rab3 subfamily GTPases.,
Methods in Molecular Biology, Vol.189, 143-156, 2002.

(キーワード): Animals / Brain / Chromatography, Thin Layer / GTPase-Activating Proteins / Guanine Nucleotide Dissociation Inhibitors / Guanine Nucleotide Exchange Factors / Rats / Recombinant Fusion Proteins / Spodoptera / rab3 GTP-Binding Proteins
(出版サイトへのリンク): ● Publication site (DOI): 10.1385/1-59259-281-3:143
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 12094583; ● Search Scopus @ Elsevier (PMID): 12094583; ● Search Scopus @ Elsevier (DOI): 10.1385/1-59259-281-3:143

(DOI: 10.1385/1-59259-281-3:143, PubMed: 12094583) Miki Tanaka, Jun Miyoshi, Hiroyoshi Ishizaki, Atsushi Togawa, Katsunori Ohnishi, Katsuaki Endo, Kaho Matsubara, Akira Mizoguchi, Takashi Nagano, Makoto Sato, Takuya Sasaki and Yoshimi Takai :
Role of Rab3 GDP/GTP exchange protein in synaptic vesicle trafficking at the mouse neuromuscular junction,
Molecular Biology of the Cell, Vol.12, No.5, 1421-1430, 2001.

(要約): The Rab3 small G protein family consists of four members, Rab3A, -3B, -3C, and -3D. Of these members, Rab3A regulates Ca(2+)-dependent neurotransmitter release. These small G proteins are activated by Rab3 GDP/GTP exchange protein (Rab3 GEP). To determine the function of Rab3 GEP during neurotransmitter release, we have knocked out Rab3 GEP in mice. Rab3 GEP-/- mice developed normally but died immediately after birth. Embryos at E18.5 showed no evoked action potentials of the diaphragm and gastrocnemius muscles in response to electrical stimulation of the phrenic and sciatic nerves, respectively. In contrast, axonal conduction of the spinal cord and the phrenic nerve was not impaired. Total numbers of synaptic vesicles, especially those docked at the presynaptic plasma membrane, were reduced at the neuromuscular junction approximately 10-fold compared with controls, whereas postsynaptic structures and functions appeared normal. Thus, Rab3 GEP is essential for neurotransmitter release and probably for formation and trafficking of the synaptic vesicles.
(キーワード): Action Potentials / Animals / Calcium-Binding Proteins / Electromyography / Embryo, Mammalian / Embryonic and Fetal Development / Female / Gene Targeting / Lung / Membrane Glycoproteins / Mice / Mice, Knockout / Microscopy, Fluorescence / Nerve Tissue Proteins / Neurofilament Proteins / Neuromuscular Junction / Receptors, Cholinergic / Synaptic Vesicles / Synaptotagmins / rab3 GTP-Binding Proteins
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 11359932; ● Summary page in Scopus @ Elsevier: 2-s2.0-0034768921

(PubMed: 11359932, Elsevier: Scopus) Yoshimi Takai, Takuya Sasaki and Takashi Matozaki :
Small GTP-binding proteins.,
Physiol. Rev., Vol.81, No.1, 153-208, 2001. F. Nagano, Takuya Sasaki and Y. Takai :
Purification and properties of Rab3 GTPase activating protein.,
Methods in Enzymology, Vol.329, 67-75, 2001.

(キーワード): Animals / Brain / Chromatography, Agarose / Chromatography, Thin Layer / Durapatite / Escherichia coli / GTPase-Activating Proteins / Lipid Metabolism / Lipids / Plasmids / Rats / Recombinant Fusion Proteins / Substrate Specificity / rab3 GTP-Binding Proteins
(出版サイトへのリンク): ● Publication site (DOI): 10.1016/S0076-6879(01)29067-3
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 11210574; ● Search Scopus @ Elsevier (PMID): 11210574; ● Search Scopus @ Elsevier (DOI): 10.1016/S0076-6879(01)29067-3

(DOI: 10.1016/S0076-6879(01)29067-3, PubMed: 11210574) H. Shirataki, Takuya Sasaki and Y. Takai :
Rabphilin-3: a target molecule for Rab3 small G proteins.,
Methods in Enzymology, Vol.329, 75-82, 2001.

(キーワード): Actin Cytoskeleton / Actinin / Adaptor Proteins, Signal Transducing / Animals / Endocytosis / Escherichia coli / Hemagglutinins / Membrane Proteins / Nerve Tissue Proteins / PC12 Cells / Protein Binding / Rats / Recombinant Fusion Proteins / Sepharose / Spodoptera / Vesicular Transport Proteins / rab GTP-Binding Proteins
(出版サイトへのリンク): ● Publication site (DOI): 10.1016/S0076-6879(01)29068-5
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 11210575; ● Search Scopus @ Elsevier (PMID): 11210575; ● Search Scopus @ Elsevier (DOI): 10.1016/S0076-6879(01)29068-5

(DOI: 10.1016/S0076-6879(01)29068-5, PubMed: 11210575) Satoshi Orita, Takuya Sasaki and Yoshimi Takai :
Doc2a as a modulator of Ca²⁺-dependent exocytosis.,
Methods in Enzymology, Vol.329, 83-90, 2001.

(キーワード): Animals / カルシウム (calcium) / Calcium-Binding Proteins / Cell-Free System / 大腸菌 (Escherichia coli) / Exocytosis / Growth Hormone / Nerve Tissue Proteins / PC12 Cells / カリウム (potassium) / Precipitin Tests / Protein Binding / Protein Structure, Tertiary / Rats / Recombinant Fusion Proteins / Tetradecanoylphorbol Acetate / Transfection
(出版サイトへのリンク): ● Publication site (DOI): 10.1016/S0076-6879(01)29069-7
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 11210576; ● Search Scopus @ Elsevier (PMID): 11210576; ● Search Scopus @ Elsevier (DOI): 10.1016/S0076-6879(01)29069-7

(DOI: 10.1016/S0076-6879(01)29069-7, PubMed: 11210576) H Ishizaki, J Miyoshi, H Kamiya, A Togawa, M Tanaka, Takuya Sasaki, K Endo, A Mizoguchi, S Ozawa and Y Takai :
Role of Rab GDP dissociation inhibitor alpha in regulating plasticity of hippocampla neurotransmission,
Proceedings of the National Academy of Sciences of the United States of America, Vol.97, No.21, 11587-11592, 2000.

(要約): Rab GDP dissociation inhibitor alpha (Rab GDIalpha) is a regulator of the Rab small G proteins implicated in neurotransmission, and mutations of Rab GDIalpha cause human X-linked mental retardation associated with epileptic seizures. In Rab GDIalpha-deficient mice, synaptic potentials in the CA1 region of the hippocampus displayed larger enhancement during repetitive stimulation, which was apparently opposite to the phenotype of Rab3A-deficient mice. Furthermore, the Rab GDIalpha-deficient mice showed hypersensitivity to bicuculline, an inducer of epileptic seizures. These results suggest that Rab GDIalpha plays a specialized role in Rab3A recycling to suppress hyperexcitability via modulation of presynaptic forms of plasticity.
(キーワード): Animals / Base Sequence / DNA Primers / Dizocilpine Maleate / Excitatory Amino Acid Antagonists / GABA Antagonists / Guanine Nucleotide Dissociation Inhibitors / Hippocampus / Humans / Mice / Mice, Inbred C57BL / N-Methylaspartate / Neuronal Plasticity / Seizures / Subcellular Fractions / Synaptic Transmission / rab3 GTP-Binding Proteins
(出版サイトへのリンク): ● Publication site (DOI): 10.1073/pnas.97.21.11587
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 11027356; ● Summary page in Scopus @ Elsevier: 2-s2.0-12944333135

(DOI: 10.1073/pnas.97.21.11587, PubMed: 11027356, Elsevier: Scopus) Toshihiko Suzuki, Hitomi Mimuro, Hiroaki Miki, Tadaomi Takenawa, Takuya Sasaki, i Hiroyuki Nakanish, Yoshimi Takai and Chihiro Sasakawa :
Rho Family GTPase Cdc42 Is Essential for the Actin-based Motility of Shigella in Mammalian Cells.,
The Journal of Experimental Medicine, Vol.191, No.11, 1905-1920, 2000.

(要約): Shigella, the causative agent of bacillary dysentery, is capable of directing its movement within host cells by exploiting actin dynamics. The VirG protein expressed at one pole of the bacterium can recruit neural Wiskott-Aldrich syndrome protein (N-WASP), a downstream effector of Cdc42. Here, we show that Cdc42 is required for the actin-based motility of Shigella. Microinjection of a dominant active mutant Cdc42, but not Rac1 or RhoA, into Swiss 3T3 cells accelerated Shigella motility. In add-back experiments in Xenopus egg extracts, addition of a guanine nucleotide dissociation inhibitor for the Rho family, RhoGDI, greatly diminished the bacterial motility or actin assembly, which was restored by adding activated Cdc42. In N-WASP-depleted extracts, the bacterial movement almost arrested was restored by adding exogenous N-WASP but not H208D, an N-WASP mutant defective in binding to Cdc42. In pyrene actin assay, Cdc42 enhanced VirG-stimulating actin polymerization by N-WASP-actin-related protein (Arp)2/3 complex. Actually, Cdc42 stimulated actin cloud formation on the surface of bacteria expressing VirG in a solution containing N-WASP, Arp2/3 complex, and G-actin. Immunohistological study of Shigella-infected cells expressing green fluorescent protein-tagged Cdc42 revealed that Cdc42 accumulated by being colocalized with actin cloud at one pole of intracellular bacterium. Furthermore, overexpression of H208D mutant in cells interfered with the actin assembly of infected Shigella and diminished the intra- and intercellular spreading. These results suggest that Cdc42 activity is involved in initiating actin nucleation mediated by VirG-N-WASP-Arp2/3 complex formed on intracellular Shigella.
(キーワード): 3T3 Cells / Actins / Animals / Bacterial Proteins / COS Cells / DNA-Binding Proteins / Dogs / Guanine Nucleotide Dissociation Inhibitors / Humans / Mammals / Mice / Microinjections / Nerve Tissue Proteins / Ovum / Rabbits / Rats / Shigella flexneri / Transcription Factors / Wiskott-Aldrich Syndrome Protein, Neuronal / Xenopus / cdc42 GTP-Binding Protein / rho Guanine Nucleotide Dissociation Inhibitor alpha / rho-Specific Guanine Nucleotide Dissociation Inhibitors
(出版サイトへのリンク): ● Publication site (DOI): 10.1084/jem.191.11.1905
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 10839806; ● Summary page in Scopus @ Elsevier: 2-s2.0-0034608674

(DOI: 10.1084/jem.191.11.1905, PubMed: 10839806, Elsevier: Scopus) Akiko Mammoto, Takuya Sasaki, Yongman Kim and Yoshimi Takai :
Physical and Functional Interaction of Rabphilin-11 with Mammalian Sec13 Protein.,
The Journal of Biological Chemistry, Vol.275, No.18, 13167-13170, 2000.

(要約): Rab11a small G protein (Rab11p) is implicated in vesicle trafficking, especially vesicle recycling. We have previously isolated a downstream effector of Rab11p, named rabphilin-11. We found here that rabphilin-11 directly bound the mammalian counterpart of yeast Sec13 protein (mSec13p) in cell-free and intact cell systems. Yeast Sec13p is involved as a component of coat proteins II in the Sar1p-induced vesicle formation from the endoplasmic reticulum, but the precise role of mSec13p is unknown. The interaction of rabphilin-11 with mSec13p was enhanced by GTP-Rab11p. Rabphilin-11 localized on the vesicles in perinuclear regions and along microtubules oriented toward the plasma membrane, whereas mSec13p partly colocalized with rabphilin-11 in the perinuclear regions, most presumably the Golgi complex. Disruption of the rabphilin-11-mSec13p interaction by overexpression of the mSec13p-binding region of rabphilin-11 impaired vesicle trafficking. These results indicate that the rabphilin-11-mSec13p interaction is implicated in vesicle trafficking.
(キーワード): Animals / Biological Transport / Cytoplasmic Granules / Fungal Proteins / Mammals / Membrane Proteins / Nuclear Pore Complex Proteins / Protein Binding / Saccharomyces cerevisiae Proteins / rab GTP-Binding Proteins
(出版サイトへのリンク): ● Publication site (DOI): 10.1074/jbc.C000096200
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 10747849; ● Summary page in Scopus @ Elsevier: 2-s2.0-0034607642

(DOI: 10.1074/jbc.C000096200, PubMed: 10747849, Elsevier: Scopus) Akiko Mammoto, Kazoo Takahashi, Takuya Sasaki and Yoshimi Takai :
Stimulation of Rho GDI release by ERM proteins.,
Methods in Enzymology, Vol.325, 91-101, 2000.

(キーワード): Binding Sites / Blood Proteins / Cytoskeletal Proteins / Guanine Nucleotide Dissociation Inhibitors / Guanosine Diphosphate / Guanosine Triphosphate / Membrane Proteins / Peptide Fragments / Protein Binding / Protein Isoforms / Recombinant Fusion Proteins / rho-Specific Guanine Nucleotide Dissociation Inhibitors / rhoA GTP-Binding Protein
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 11036595; ● Summary page in Scopus @ Elsevier: 2-s2.0-0033780416

(PubMed: 11036595, Elsevier: Scopus) G. Sakaguchi, T. Manabe, K. Kobayashi, S. Orita, Takuya Sasaki, A. Naito, M. Maeda, H. Igarashi, G. Katsuura, H. Nishioka, A. Mizoguchi, S. Itohara, T. Takahashi and Y. Takai :
Doc2 is an activity-dependent presynaptic modulator of neurotransmitter release.,
Eur. J. Neurosci., Vol.11, No.12, 4262-4268, 1999. T. Asakura, H. Nakanishi, T. Sakisaka, K. Takahashi, K. Mandai, M. Nishimura, Takuya Sasaki and Y. Takai :
Similar and differential behavior between the nectin-afadin-ponsin and cadherin-catenin systems during the formation and disruption of the polarized junctional alignment in epithelial cells.,
Genes to Cells, Vol.4, No.10, 573-581, 1999.

(要約): We have recently identified a novel cell-cell adhesion system, named NAP system, which is localized at cadherin-based cell-cell adherens junctions (AJs). The NAP system is composed of at least nectin, afadin and ponsin. Nectin is an immunoglobulin-like cell adhesion molecule. Afadin is an actin filament-binding protein which associates nectin with the actin cytoskeleton. Ponsin is an afadin-binding protein which furthermore binds to vinculin and provides a possible linkage of nectin-afadin to cadherin-catenin through vinculin. We compared here the behaviour of the NAP and cadherin-catenin systems during the formation and disruption of the polarized junctional alignment in epithelial cells. At the early stage of the formation of the polarized junctional alignment in MTD-1 A cells, primordial spot-like junctions were formed at the tips of thin cellular protrusions radiating from adjacent cells. Nectin, afadin, ponsin, cadherin and catenin were simultaneously recruited to these junctions. As the cell polarization proceeded, the spot-like junctions were gradually fused to form belt-like AJs where all these proteins were concentrated. The disruption of cell-cell AJs in MDCK cells by culturing at a low Ca2+ concentration caused rapid endocytosis of cadherin, but not that of nectin or afadin. Addition of 12-O-tetradecanoylphorbol-13-acetate to the cells formed a tight junction-like structure where nectin and afadin, but not cadherin, accumulated. These results indicate that the NAP and cadherin-catenin systems show similar and differential behaviour during the formation and disruption of the polarized junctional alignment in epithelial cells.
(キーワード): Animals / Cadherins / Cell Adhesion / Cell Adhesion Molecules / Cell Line / Epithelial Cells / Humans / Immunoglobulins / Intercellular Junctions / Kinesin / Mice / Microfilament Proteins / Microscopy, Fluorescence / Myosins / Rabbits
(出版サイトへのリンク): ● Publication site (DOI): 10.1046/j.1365-2443.1999.00283.x
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 10583506; ● Search Scopus @ Elsevier (PMID): 10583506; ● Search Scopus @ Elsevier (DOI): 10.1046/j.1365-2443.1999.00283.x

(DOI: 10.1046/j.1365-2443.1999.00283.x, PubMed: 10583506) A Mammoto, T Ohtsuka, I Hotta, Takuya Sasaki and Y Takai :
Rab11BP/Rabphilin-11 A dodwnstream target of rab11 small G protein implicated in vesicle recycling,
The Journal of Biological Chemistry, Vol.274, No.36, 25517-25524, 1999.

(要約): Rab11 small G protein has been implicated in vesicle recycling, but its upstream regulators or downstream targets have not yet been identified. We isolated here a downstream target of Rab11, named rabphilin-11, from bovine brain. Moreover, we isolated from a rat brain cDNA library its cDNA, which encoded a protein with a M(r) of 100,946 and 908 amino acids (aa). Rabphilin-11 bound GTP-Rab11 more preferentially than GDP-Rab11 at the N-terminal region and was specific for Rab11 and inactive for other Rab and Rho small G proteins. Both GTP-Rab11 and rabphilin-11 were colocalized at perinuclear regions, presumably the Golgi complex and recycling endosomes, in Madin-Darby canine kidney cells. In HeLa cells cultured on fibronectin, both the proteins were localized not only at perinuclear regions but also along microtubules, which were oriented toward membrane lamellipodia. Treatment of HeLa cells with nocodazole caused disruption of microtubules and dispersion of GTP-Rab11 and rabphilin-11. Overexpression of the C-terminal fragment of rabphilin-11 (aa 607-730), lacking the GTP-Rab11 binding domain, in HeLa cells reduced accumulation of transferrin at perinuclear regions and cell migration. Rabphilin-11 turned out to be a rat counterpart of recently reported bovine Rab11BP. These results indicate that rabphilin-11 is a downstream target of Rab11 which is involved in vesicle recycling.
(キーワード): Amino Acid Sequence / Animals / Antineoplastic Agents / Biological Transport / Cattle / Cytoplasmic Granules / Dogs / GTP-Binding Proteins / HeLa Cells / Humans / Microtubules / Molecular Sequence Data / Nocodazole / Rats / rab GTP-Binding Proteins
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 10464283; ● Search Scopus @ Elsevier (PMID): 10464283

(PubMed: 10464283) G Sakaguchi, T Manabe, K Kobayashi, Satoshi Orita and Takuya Sasaki :
Doc2 is an activity-dependent modulator of excitatory synaptic transmission.,
Eur. J. Neurosci., Vol.11, No.1, 4262-4268, 1999. H. Oishi, Takuya Sasaki, F. Nagano, W. Ikeda, T. Ohya, M. Wada, N. Ide, H. Nakanishi and Y. Takai :
Localization of the Rab3 small G protein regulators in nerve terminals and their involvement in Ca²⁺-dependent exocytosis.,
The Journal of Biological Chemistry, Vol.273, No.51, 34580-34585, 1998.

(要約): The Rab3 small G protein subfamily (Rab3) consists of four members, Rab3A, -B, -C, and -D. We have recently isolated and characterized the Rab3 regulators, GDP/GTP exchange protein (GEP) and GTPase activating protein (GAP), both of which are specific for the Rab3 subfamily. Rab3 GEP stimulates the conversion of the GDP-bound inactive form to the GTP-bound active form, whereas Rab3 GAP stimulates the reverse reaction. Of the four members of the Rab3 subfamily, evidence is accumulating that Rab3A is involved in Ca2+-dependent exocytosis, particularly in neurotransmitter release. We first analyzed the subcellular localization of Rab3 GEP and GAP in rat brain. Subcellular fractionation analysis showed that both Rab3 GEP and GAP were enriched in the synaptic soluble fraction. Immunocytochemical analysis in primary cultured rat hippocampal neurons showed that both Rab3 GEP and GAP were concentrated at the presynaptic nerve terminals. We then examined whether Rab3 GEP and GAP were involved in Ca2+-dependent exocytosis by use of human growth hormone (GH) co-expression assay system of cultured PC12 cells. Overexpression of the deletion mutant of Rab3 GEP possessing the catalytic activity reduced the high K+-induced GH release without affecting the basal GH release, whereas that of the deletion mutant lacking the catalytic activity showed no effect on the high K+-induced GH release. In contrast, overexpression of Rab3 GAP or its deletion mutant possessing the catalytic activity did not affect the high K+-induced GH release or the basal GH release. These results indicate that Rab3 GEP and GAP are colocalized with Rab3A at the synaptic release sites and suggest that they regulate the activity of Rab3A and are involved in Ca2+-dependent exocytosis.
(キーワード): Animals / Brain / Calcium / Exocytosis / GTP-Binding Proteins / GTPase-Activating Proteins / Growth Hormone / Guanine Nucleotide Exchange Factors / Hippocampus / Humans / Nerve Tissue Proteins / Neurons / PC12 Cells / Presynaptic Terminals / Proteins / Rabbits / Rats / Recombinant Proteins / Spodoptera / Transfection / rab3 GTP-Binding Proteins
(出版サイトへのリンク): ● Publication site (DOI): 10.1074/jbc.273.51.34580
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 9852129; ● Search Scopus @ Elsevier (PMID): 9852129; ● Search Scopus @ Elsevier (DOI): 10.1074/jbc.273.51.34580

(DOI: 10.1074/jbc.273.51.34580, PubMed: 9852129) F. Nagano, Satoshi Orita, Takuya Sasaki, A Naito and G Sakaguchi :
Interaction of Doc2 with tctex-1, a light chain of cytoplasmic dynein. Implication in dynein-dependent vesicle transport.,
The Journal of Biological Chemistry, Vol.273, No.46, 30065-30068, 1998.

(要約): Doc2 has one Munc13-interacting domain at the N-terminal region and two C2-like domains interacting with Ca2+ and phospholipid at the C-terminal region. Doc2 consists of two isoforms, Doc2alpha and -beta. Doc2alpha is specifically expressed in neuronal cells and implicated in Ca2+-dependent neurotransmitter release, whereas Doc2beta is ubiquitously expressed and its function is unknown. We show here that both Doc2alpha and -beta interact with rat tctex-1, a light chain of cytoplasmic dynein, in both cell-free and intact cell systems. Overexpression of the N-terminal fragment of Doc2 containing the tctex-1-interacting domain induces changes in the intracellular localization of cation-independent mannose 6-phosphate receptor and its ligand, cathepsin D, which are transported from trans-Golgi network to late endosomes. Overexpression of the C-terminal fragment containing two C2-like domains shows the similar effect, but to a lesser extent, whereas overexpression of full-length Doc2 or the C-terminal fragment of rabphilin3 containing two C2-like domains does not show this effect. Because dynein is a minus-end-directed microtubule-based motor protein, these results suggest that Doc2, especially Doc2beta, plays a role in dynein-dependent intracellular vesicle transport.
(キーワード): Amino Acid Sequence / Animals / Base Sequence / Biological Transport / Calcium-Binding Proteins / Cathepsin D / Cricetinae / Dyneins / Humans / Microtubule Proteins / Microtubule-Associated Proteins / Molecular Sequence Data / Nerve Tissue Proteins / Nuclear Proteins / Protein Binding / Rats / Receptor, IGF Type 2 / t-Complex Genome Region
(出版サイトへのリンク): ● Publication site (DOI): 10.1074/jbc.273.46.30065
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 9804756; ● Search Scopus @ Elsevier (PMID): 9804756; ● Search Scopus @ Elsevier (DOI): 10.1074/jbc.273.46.30065

(DOI: 10.1074/jbc.273.46.30065, PubMed: 9804756) F. Nagano, S. Orita, Takuya Sasaki, A. Naito, G. Sakaguchi, M. Maeda, T. Watanabe, E. Kominami, Y. Uchiyama and Y. Takai :
Interaction of Doc2 with Tctex-1, a light chain of cytoplasmic dynein Implication in dynein-dependent vesicle transport.,
The Journal of Biological Chemistry, Vol.273, No.46, 30065-30068, 1998. F. Nagano, Takuya Sasaki, K. Fukui, T. Asakura, K. Imazumi and Y. Takai :
Molecular cloning and characterization of the noncatalytic subunit of the Rab3 subfamily-specific GTPase activating protein.,
The Journal of Biological Chemistry, Vol.273, No.38, 24781-24785, 1998. S. Mochida, S. Orita, G. Sakaguchi, Takuya Sasaki and Y. Takai :
Role of the Doc2a-Munc13-1 interaction in the neurotransmitter release process.,
Proc. Natl. Acad. Sci. USA, Vol.95, No.19, 11418-11422, 1998. H. Imamura, K. Takaishi, K. Nakano, A. Kodama, H. Oishi, H. Shiozaki, M. Monden, Takuya Sasaki and Y. Takai :
Rho and Rab small G proteins coordinately reorganize stress fibers and focal adhesions in MDCK cells.,
Molecular Biology of the Cell, Vol.9, No.9, 2561-2575, 1998.

(要約): The Rho subfamily of the Rho small G protein family (Rho) regulates formation of stress fibers and focal adhesions in many types of cultured cells. In moving cells, dynamic and coordinate disassembly and reassembly of stress fibers and focal adhesions are observed, but the precise mechanisms in the regulation of these processes are poorly understood. We previously showed that 12-O-tetradecanoylphorbol-13-acetate (TPA) first induced disassembly of stress fibers and focal adhesions followed by their reassembly in MDCK cells. The reassembled stress fibers showed radial-like morphology that was apparently different from the original. We analyzed here the mechanisms of these TPA-induced processes. Rho inactivation and activation were necessary for the TPA-induced disassembly and reassembly, respectively, of stress fibers and focal adhesions. Both inactivation and activation of the Rac subfamily of the Rho family (Rac) inhibited the TPA-induced reassembly of stress fibers and focal adhesions but not their TPA-induced disassembly. Moreover, microinjection or transient expression of Rab GDI, a regulator of all the Rab small G protein family members, inhibited the TPA-induced reassembly of stress fibers and focal adhesions but not their TPA-induced disassembly, indicating that, furthermore, activation of some Rab family members is necessary for their TPA-induced reassembly. Of the Rab family members, at least Rab5 activation was necessary for the TPA-induced reassembly of stress fibers and focal adhesions. The TPA-induced, small G protein-mediated reorganization of stress fibers and focal adhesions was closely related to the TPA-induced cell motility. These results indicate that the Rho and Rab family members coordinately regulate the TPA-induced reorganization of stress fibers and focal adhesions that may cause cell motility.
(キーワード): Actins / Animals / Cell Adhesion / Cell Line / Cytoskeleton / Dogs / GTP-Binding Proteins / Guanine Nucleotide Dissociation Inhibitors / Hepatocyte Growth Factor / Humans / Tetradecanoylphorbol Acetate / rab GTP-Binding Proteins / rab5 GTP-Binding Proteins / rac GTP-Binding Proteins / rhoA GTP-Binding Protein
(出版サイトへのリンク): ● Publication site (DOI): 10.1091/mbc.9.9.2561
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 9725912; ● Search Scopus @ Elsevier (PMID): 9725912; ● Search Scopus @ Elsevier (DOI): 10.1091/mbc.9.9.2561

(DOI: 10.1091/mbc.9.9.2561, PubMed: 9725912) Gaku Sakaguchi, Satoshi Orita, Akira Naito, Miki Maeda, Hisanaga Igarashi, Takuya Sasaki and Yoshimi Takai :
A novel brain-specific isoform of spectrin : isolation and its interaction with Munc13.,
Biochemical and Biophysical Research Communications, Vol.248, No.3, 846-851, 1998.

(要約): Munc13 is a component of the neurotransmitter release machinery which is specifically expressed in brain. Munc13 interacts with Doc2 and syntaxin which are also implicated in the neurotransmitter release process. Here we isolated another Munc13-interacting molecule from a rat brain cDNA library by use of the yeast two-hybrid system, identified it to be a novel type of beta spectrin, and named it beta SpIII sigma 1. beta SpIII sigma 1 was specifically expressed in brain, where it was enriched in the synaptic vesicle and plasma membrane fractions. Because spectrin has been shown to interact with the actin cytoskeleton which is involved in the exocytotic process, the present results suggest that the Munc13-beta SpIII sigma 1 interactions play a role in neurotransmitter release.
(キーワード): Amino Acid Sequence / Animals / Blotting, Northern / 脳 (brain) / Cell-Free System / Conserved Sequence / Gene Library / Molecular Sequence Data / Nerve Tissue Proteins / Organ Specificity / Phylogeny / Rats / Recombinant Proteins / Sequence Alignment / Sequence Homology, Amino Acid / Spectrin
(出版サイトへのリンク): ● Publication site (DOI): 10.1006/bbrc.1998.9067
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 9704016; ● Search Scopus @ Elsevier (PMID): 9704016; ● Search Scopus @ Elsevier (DOI): 10.1006/bbrc.1998.9067

(DOI: 10.1006/bbrc.1998.9067, PubMed: 9704016) K. Takahashi, Takuya Sasaki, A. Mammoto, I. Hotta, K. Takaishi, H. Imamura, K. Nakano, A. Kodama and Y. Takai :
Interaction of radixin with Rho small G protein GDP/GTP exchange protein Dbl.,
Oncogene, Vol.16, No.25, 3279-3284, 1998.

(要約): The Rho small G protein family, consisting of the Rho, Rac, and Cdc42 subfamilies, regulates various actin cytoskeleton-dependent cell functions. The Rho subfamily members regulate ERM (ezrin, radixin and moesin)-dependent association of the actin cytoskeleton with the plasma membrane. Moreover, the N-terminal regions of ERM interact with Rho GDI, an inhibitory regulator of all the Rho family members, and reduce its inhibitory action, finally initiating the activation of the Rho family members. We show here that the N-terminal region of radixin furthermore interacts with Dbl, a stimulatory GDP/GTP exchange protein of the Rho family members. This interaction does not affect the Dbl activity to stimulate the GDP/GTP exchange reaction of RhoA, a member of the Rho subfamily. Dbl does not interact with radixin which is precomplexed with Rho GDI, and Rho GDI displaces Dbl from radixin. Thus, radixin plays an important role in activation of the Rho family members by recruiting their positive and negative regulators.
(キーワード): Binding Sites / Blood Proteins / Cytoskeletal Proteins / DNA-Binding Proteins / GTP-Binding Proteins / Glutathione Transferase / Guanine Nucleotide Dissociation Inhibitors / Guanosine Diphosphate / Guanosine Triphosphate / Membrane Proteins / Peptide Fragments / Protein Binding / Retroviridae Proteins, Oncogenic / Rho Factor / Transcription Factors
(出版サイトへのリンク): ● Publication site (DOI): 10.1038/sj.onc.1201874
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 9681826; ● Search Scopus @ Elsevier (PMID): 9681826; ● Search Scopus @ Elsevier (DOI): 10.1038/sj.onc.1201874

(DOI: 10.1038/sj.onc.1201874, PubMed: 9681826) Takuya Sasaki and Y. Takai :
The rho small G protein family-rho GDI system as a temporal and spatial determinant for cytoskeletal control.,
Biochemical and Biophysical Research Communications, Vol.245, No.3, 641-645, 1998.

(要約): Recent extensive studies have clarified the functions of the small G protein superfamily, which consists of the Ras, Rho, Rab, Arf, Sar1, and Ran families (for reviews, Refs, 1 and 2). The Ras family regulates gene expression at least through the MAP kinase cascade; the Rho family mainly regulates reorganization of the actin cytoskeleton; the Rab, Arf, and Sar1 families regulate intracellular vesicle trafficking; and the Ran family regulates nuclear transport. Of these cellular functions, reorganization of the actin cytoskeleton, seen in the formation of filopodia, lamellipodia, and ruffles during cell motility, dynamically occurs at specific sites of cells. To regulate this type of dynamic cellular functions, temporal and spatial determination mechanisms of signal transduction would be important. Like other G proteins, small G proteins cycle between the GDP-bound inactive and GTP-bound active forms (1,2). They receive upstream signals through their regulators and transduce signals to downstream targets while they stay in the GTP-bound form. Thus, G proteins serve as timers. There are at least three types of regulators for small G proteins: GDP/GTP exchange protein (GEP) which stimulates conversion from the GDP-bound form to the GTP-bound form; GDP dissociation inhibitor (GDI) which inhibits this reaction; and GTPase activating protein (GAP) which stimulates conversion from the GTP-bound form to the GDP-bound form. Of these regulators, GDI has thus far been found for the Rho and Rab families. We have recently found that the Rho family-Rho GDI system plays an important role in spatial determination in the actin cytoskeletal control (3-6). We briefly describe here this function of the Rho family-Rho GDI system.
(キーワード): Animals / Cytoskeleton / DNA-Binding Proteins / GTP-Binding Proteins / Guanine Nucleotide Dissociation Inhibitors / Humans / Models, Biological / Signal Transduction / Transcription Factors / rho-Specific Guanine Nucleotide Dissociation Inhibitors
(出版サイトへのリンク): ● Publication site (DOI): 10.1006/bbrc.1998.8253
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 9588168; ● Search Scopus @ Elsevier (PMID): 9588168; ● Search Scopus @ Elsevier (DOI): 10.1006/bbrc.1998.8253

(DOI: 10.1006/bbrc.1998.8253, PubMed: 9588168) M. Umikawa, K. Tanaka, T. Kamei, K. Shimizu, H. Imamura, Takuya Sasaki and Y. Takai :
Interaction of Rho1p target Bni1p and F-Actin-binding elongation factor 1alpha - Implication in Rho1p-regulated reorganization of the actin cytoskeleton in Saccharomyces cerevisiae.,
Oncogene, Vol.16, No.15, 2011-2016, 1998.

(要約): The RHO1 gene encodes a homolog of mammalian RhoA small G protein in the yeast Saccharomyces cerevisiae. We have shown that Bni1p is one of the downstream targets of Rho1p and regulates reorganization of the actin cytoskeleton through the interaction with profilin, an actin monomer-binding protein. A Bni1p-binding protein was affinity purified from the yeast cytosol fraction and was identified to be Tef1p/Tef2p, translation elongation factor 1alpha (EF1alpha). EF1alpha is an essential component of the protein synthetic machinery and also possesses the actin filament (F-actin)-binding and -bundling activities. EF1alpha bound to the 186 amino acids region of Bni1p, located between the FH1 domain, the proline-rich profilin-binding domain, and the FH2 domain, of which function is not known. The binding of Bni1p to EF1alpha inhibited its F-actin-binding and -bundling activities. The BNI1 gene deleted in the EF1alpha-binding region did not suppress the bni1 bnr1 mutation in which the actin organization was impaired. These results suggest that the Rho1p-Bni1p system regulates reorganization of the actin cytoskeleton through the interaction with both EF1alpha and profilin.
(キーワード): Actins / Binding Sites / Carrier Proteins / Cytoskeleton / Fungal Proteins / GTP-Binding Proteins / Membrane Proteins / Microfilament Proteins / Peptide Elongation Factor 1 / Peptide Elongation Factors / Saccharomyces cerevisiae / Saccharomyces cerevisiae Proteins / rhoB GTP-Binding Protein
(出版サイトへのリンク): ● Publication site (DOI): 10.1038/sj.onc.1201724
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 9591785; ● Search Scopus @ Elsevier (PMID): 9591785; ● Search Scopus @ Elsevier (DOI): 10.1038/sj.onc.1201724

(DOI: 10.1038/sj.onc.1201724, PubMed: 9591785) A. Mammoto, Takuya Sasaki, T. Asakura, I. Hotta, H. Imamura, K. Takahashi, Y. Matsuura, T. Shirao and Y. Takai :
Interactions of drebrin and gephyrin with profilin.,
Biochemical and Biophysical Research Communications, Vol.243, No.1, 86-89, 1998.

(要約): Profilin is an actin monomer-binding protein which stimulates actin polymerization. Recent studies have revealed that profilin interacts with VASP, Mena, Bnilp, Bnrlp, and mDia, all of which have the proline-rich domain. Here, we isolated three profilin-binding proteins from rat brain cytosol by glutathione S-transferase-profilin affinity column chromatography and identified them as Mena, drebrin, and gephyrin. These proteins had a proline-rich domain and directly interacted with profilin.
(キーワード): Amino Acid Sequence / Animals / Binding Sites / Brain / Carrier Proteins / Contractile Proteins / Cytosol / Humans / In Vitro Techniques / Membrane Proteins / Microfilament Proteins / Molecular Sequence Data / Neuropeptides / Peptide Mapping / Profilins / Proline / Protein Binding / Rats / Recombinant Fusion Proteins
(出版サイトへのリンク): ● Publication site (DOI): 10.1006/bbrc.1997.8068
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 9473484; ● Search Scopus @ Elsevier (PMID): 9473484; ● Search Scopus @ Elsevier (DOI): 10.1006/bbrc.1997.8068

(DOI: 10.1006/bbrc.1997.8068, PubMed: 9473484) M.E. Burns, Takuya Sasaki, Y. Takai and G.J. Augustine :
Rabphilin-3A : a multifunctional regulator of synaptic vesicle traffic.,
The Journal of General Physiology, Vol.111, No.2, 243-255, 1998.

(要約): We have investigated the function of the synaptic vesicle protein Rabphilin-3A in neurotransmitter release at the squid giant synapse. Presynaptic microinjection of recombinant Rabphilin-3A reversibly inhibited the exocytotic release of neurotransmitter. Injection of fragments of Rabphilin-3A indicate that at least two distinct regions of the protein inhibit neurotransmitter release: the NH2-terminal region that binds Rab3A and is phosphorylated by protein kinases and the two C2 domains that interact with calcium, phospholipid, and beta-adducin. Each of the inhibitory fragments and the full-length protein had separate effects on presynaptic morphology, suggesting that individual domains were inhibiting a subset of the reactions in which the full-length protein participates. In addition to inhibiting exocytosis, constructs containing the NH2 terminus of Rabphilin-3A also perturbed the endocytotic pathway, as indicated by changes in the membrane areas of endosomes, coated vesicles, and the plasma membrane. These results indicate that Rabphilin-3A regulates synaptic vesicle traffic and appears to do so at distinct stages of both the exocytotic and endocytotic pathways.
(キーワード): Adaptor Proteins, Signal Transducing / Animals / Cell Membrane / Decapodiformes / Electrophysiology / Endocytosis / Exocytosis / GTP-Binding Proteins / Ganglia, Invertebrate / In Vitro Techniques / Microinjections / Microscopy, Electron / Nerve Tissue Proteins / Neurotransmitter Agents / Recombinant Proteins / Stellate Ganglion / Synaptic Vesicles / Vesicular Transport Proteins / rab GTP-Binding Proteins
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 9450942; ● Search Scopus @ Elsevier (PMID): 9450942

(PubMed: 9450942) T. Asakura, Takuya Sasaki, F. Nagano, A. Satoh, H. Obaishi, H. Nishioka, H. Imamura, K. Hotta, K. Tanaka, H. Nakanishi and Y. Takai :
Isolation and characterization of a novel actin filament-binding protein from Saccharomyces cerevisiae.,
Oncogene, Vol.16, No.1, 121-130, 1998.

(要約): We purified a novel actin filament (F-actin)-binding protein from the soluble fraction of Saccharomyces cerevisiae by successive column chromatographies by use of the 125I-labeled F-actin blot overlay method. The purified protein showed a minimum Mr of about 140 kDa on SDS-polyacrylamide gel electrophoresis and we named it ABP140. A search with the partial amino acid sequences of ABP140 against the Saccharomyces Genome Database revealed that the open reading frame of the ABP140 gene (ABP140) corresponded to YOR239W fused with YOR240W by the +1 translational frame shift. The encoded protein consisted of 628 amino acids with a calculated Mr of 71,484. The recombinant protein interacted with F-actin and showed the activity to crosslink F-actin into a bundle. Indirect immunofluorescence study demonstrated that ABP140 was colocalized with both cortical actin patches and cytoplasmic actin cables in intact cells. However, elimination of ABP140 by gene disruption did not show a deleterious effect on cell growth or affect the organization of F-actin. These results indicate that ABP140 is not required for cell growth but may be involved in the reorganization of F-actin in the budding yeast.
(キーワード): Actins / Amino Acid Sequence / Base Sequence / Cytosol / Microfilament Proteins / Molecular Sequence Data / Open Reading Frames / Peptide Mapping / Recombinant Proteins / Saccharomyces cerevisiae / Saccharomyces cerevisiae Proteins
(出版サイトへのリンク): ● Publication site (DOI): 10.1038/sj.onc.1201487
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 9467951; ● Search Scopus @ Elsevier (PMID): 9467951; ● Search Scopus @ Elsevier (DOI): 10.1038/sj.onc.1201487

(DOI: 10.1038/sj.onc.1201487, PubMed: 9467951) T. Ohya, Takuya Sasaki, M. Kato and Y. Takai :
Involvement of Rabphilin3 in endocytosis through interaction with Rabaptin5.,
The Journal of Biological Chemistry, Vol.273, No.1, 613-617, 1998. H. Miki, Takuya Sasaki, Y. Takai and T. Takenawa :
Induction of filopodium formation by a WASP-related actin-depolymerizing protein N-WASP.,
Nature, Vol.391, No.6662, 93-96, 1998.

(要約): Cdc42 is a small GTPase of the Rho family which regulates the formation of actin filaments to generate filopodia. Although there are several proteins such as PAK, ACK and WASP (Wiskott-Aldrich syndrome protein) that bind Cdc42 directly, none of these can account for the filopodium formation induced by Cdc42. Here we demonstrate that before it can induce filopodium formation, Cdc42 must bind a WASP-related protein, N-WASP, that is richest in neural tissues but is expressed ubiquitously. N-WASP induces extremely long actin microspikes only when co-expressed with active Cdc42, whereas WASP, which is expressed in haematopoietic cells, does not, despite the structural similarities between WASP and N-WASP. In a cell-free system, addition of active Cdc42 significantly stimulates the actin-depolymerizing activity of N-WASP, creating free barbed ends from which actin polymerization can then take place. This activation seems to be caused by exposure of N-WASP's actin-depolymerizing region induced by Cdc42 binding.
(キーワード): 3T3 Cells / Actins / Animals / Biopolymers / COS Cells / Cell Cycle Proteins / Cell Membrane / GTP-Binding Proteins / Humans / Mice / Mutation / Nerve Tissue Proteins / Organelles / Proteins / Rats / Wiskott-Aldrich Syndrome Protein / Wiskott-Aldrich Syndrome Protein, Neuronal / cdc42 GTP-Binding Protein
(出版サイトへのリンク): ● Publication site (DOI): 10.1038/34208
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 9422512; ● Search Scopus @ Elsevier (PMID): 9422512; ● Search Scopus @ Elsevier (DOI): 10.1038/34208

(DOI: 10.1038/34208, PubMed: 9422512) S Mochida, Satoshi Orita, G. Sakaguchi, Takuya Sasaki and Y. Takai :
Role of the Doc2 alpha-Munc13-1 interaction in the neurotransmitter release process.,
Proc. Natl. Acad. Sci. USA, Vol.95, 11418-11422, 1998. K. Takaishi, Takuya Sasaki, H. Kotani, H. Nishioka and Y. Takai :
Regulation of cell-cell adhesion by Rac and Rho small G proteins in MDCK cells.,
The Journal of Cell Biology, Vol.139, No.4, 1047-1059, 1997.

(要約): The Rho small G protein family, consisting of the Rho, Rac, and Cdc42 subfamilies, regulates various cell functions, such as cell shape change, cell motility, and cytokinesis, through reorganization of the actin cytoskeleton. We show here that the Rac and Rho subfamilies furthermore regulate cell-cell adhesion. We prepared MDCK cell lines stably expressing each of dominant active mutants of RhoA (sMDCK-RhoDA), Rac1 (sMDCK-RacDA), and Cdc42 (sMDCK-Cdc42DA) and dominant negative mutants of Rac1 (sMDCK-RacDN) and Cdc42 (sMDCK-Cdc42DN) and analyzed cell adhesion in these cell lines. The actin filaments at the cell-cell adhesion sites markedly increased in sMDCK-RacDA cells, whereas they apparently decreased in sMDCK-RacDN cells, compared with those in wild-type MDCK cells. Both E-cadherin and beta-catenin, adherens junctional proteins, at the cell-cell adhesion sites also increased in sMDCK-RacDA cells, whereas both of them decreased in sMDCK-RacDN cells. The detergent solubility assay indicated that the amount of detergent-insoluble E-cadherin increased in sMDCK-RacDA cells, whereas it slightly decreased in sMDCK-RacDN cells, compared with that in wild-type MDCK cells. In sMDCK-RhoDA, -Cdc42DA, and -Cdc42DN cells, neither of these proteins at the cell-cell adhesion sites was apparently affected. ZO-1, a tight junctional protein, was not apparently affected in any of the transformant cell lines. Electron microscopic analysis revealed that sMDCK-RacDA cells tightly made contact with each other throughout the lateral membranes, whereas wild-type MDCK and sMDCK-RacDN cells tightly and linearly made contact at the apical area of the lateral membranes. These results suggest that the Rac subfamily regulates the formation of the cadherin-based cell- cell adhesion. Microinjection of C3 into wild-type MDCK cells inhibited the formation of both the cadherin-based cell-cell adhesion and the tight junction, but microinjection of C3 into sMDCK-RacDA cells showed little effect on the localization of the actin filaments and E-cadherin at the cell-cell adhesion sites. These results suggest that the Rho subfamily is necessary for the formation of both the cadherin-based cell- cell adhesion and the tight junction, but not essential for the Rac subfamily-regulated, cadherin-based cell- cell adhesion.
(キーワード): Actins / Animals / Cadherins / Cell Adhesion / Cell Cycle Proteins / Cell Line / Cell Size / Cytoskeletal Proteins / Cytoskeleton / Dogs / Fluorescent Antibody Technique, Indirect / GTP-Binding Proteins / Immunohistochemistry / Membrane Proteins / Microscopy, Electron / Phosphoproteins / Solubility / Trans-Activators / Transfection / Zonula Occludens-1 Protein / beta Catenin / cdc42 GTP-Binding Protein / rac GTP-Binding Proteins / rho GTP-Binding Proteins
(出版サイトへのリンク): ● Publication site (DOI): 10.1083/jcb.139.4.1047
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 9362522; ● Search Scopus @ Elsevier (PMID): 9362522; ● Search Scopus @ Elsevier (DOI): 10.1083/jcb.139.4.1047

(DOI: 10.1083/jcb.139.4.1047, PubMed: 9362522) K. Takahashi, Takuya Sasaki, A. Mammoto, K. Takaishi, T. Kameyama, Sa. Tsukita, Sh. Tsukita and Y. Takai :
Direct interaction of the Rho GDP dissociation inhibitor with ezrin/radixin/moesin initiates the activation of the Rho small G protein.,
The Journal of Biological Chemistry, Vol.272, No.37, 23371-23375, 1997. S. Orita, A. Naito, G. Sakaguchi, M. Maeda, H. Igarashi, Takuya Sasaki and Y. Takai :
Physical and functional interactions of Doc2 and Munc13 in Ca²⁺ -dependent exocytotic machinery.,
The Journal of Biological Chemistry, Vol.272, No.26, 16081-16084, 1997. M. Wada, K. Fukui, Takuya Sasaki, K. Imazumi, Y. Matsuura, H. Nakanishi and Y. Takai :
Rab, GAP and GEP make three.,
Trends Cell Biol., Vol.7, No.5, 180, 1997. H. Kotani, K. Takaishi, Takuya Sasaki and Y. Takai :
Rho regulates association of both the ERM family and vinculin with the plasma membrane in MDCK cells.,
Oncogene, Vol.14, No.14, 1705-1713, 1997. A. Naito, S. Orita, A. Wanaka, Takuya Sasaki, G. Sakaguchi, M. Maeda, H. Igarashi, M. Tohyama and Y. Takai :
Molecular cloning of mouse Doc2alpha and distribution of its mRNA in adult mouse brain.,
Brain Res. Mol. Brain Res., Vol.44, No.2, 198-204, 1997. K. Fukui, Takuya Sasaki, K. mazumi, Y. Matsuura, H. Nakanishi and Y. Takai :
Isolation and characterization of a GTPase activating protein specific for the Rab3 subfamily of small G proteins.,
The Journal of Biological Chemistry, Vol.272, No.8, 4655-4658, 1997. A. Naito, Satoshi Orita, A. Wanaka, Takuya Sasaki and G Sakaguchi :
Moclecular cloning of mouse Doc2and distribution of its mRNA in adult mouse brain.,
Mol. Brain Res.,, Vol.44, 198-204, 1997. M. Kato, Takuya Sasaki, T. Ohya, H. Nakanishi, H. Nishioka, M. Imamura and Y. Takai :
Physical and functional interaction of Rabphilin-3A with alpha-Actinin.,
The Journal of Biological Chemistry, Vol.271, No.50, 31775-31778, 1996. H. Oishi, Takuya Sasaki and Y. Takai :
Interaction of both the C2A and C2B domains of rabphilin3 with Ca²⁺ and pospholipid.,
Biochemical and Biophysical Research Communications, Vol.229, No.2, 498-503, 1996. N. Masumoto, Takuya Sasaki, M. Tahara, A. Mammoto, Y. Ikebuchi, K. Tasaka, M. Tokunaga, Y. Takai and A. Miyake :
Involvement of Rabphilin-3A in cortical granule exocytosis in mouse eggs.,
The Journal of Cell Biology, Vol.135, No.6 Pt 2, 1741-1747, 1996.

(要約): Rabphilin-3A is a putative target protein for Rab3A, a member of the small GTP-binding protein superfamily that has been suggested to play a role in regulated exocytosis in presynapses. In this study we determined the expression and the function of Rabphilin-3A in mouse eggs at fertilization. Rabphilin-3A mRNA and protein were detected by reverse transcriptase-PCR and immunoblot analysis, respectively, in metaphase II mouse eggs. Immunofluorescence analysis showed that Rabphilin-3A protein was distributed in the cortical region in eggs. Sperm induces cortical granule (CG) exocytosis via an increase in cytosolic Ca2+ at fertilization. We microinjected the NH2- or COOH-terminal fragment of recombinant Rabphilin-3A into metaphase II eggs. Neither treatments altered the sperm-induced cytosolic Ca2+ increase, but both inhibited CG exocytosis in a dose-dependent manner. The NH2-terminal fragment was more effective than the COOH-terminal fragment. Full-length Rabphilin-3A did not affect CG exocytosis, but it attenuated the inhibition of CG exocytosis by the NH2-terminal fragment. These results show that Rabphilin-3A is involved in Ca(2+)-dependent CG exocytosis at fertilization in mouse eggs.
(キーワード): Adaptor Proteins, Signal Transducing / Animals / Calcium / Cytoplasmic Granules / Exocytosis / Female / Fertilization / GTP-Binding Proteins / Gene Expression / Glutathione Transferase / Hemagglutinins / Male / Metaphase / Mice / Mice, Inbred Strains / Molecular Sequence Data / Nerve Tissue Proteins / Ovum / Peptide Fragments / RNA, Messenger / Signal Transduction / Vesicular Transport Proteins / rab GTP-Binding Proteins
(出版サイトへのリンク): ● Publication site (DOI): 10.1083/jcb.135.6.1741
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 8991087; ● Search Scopus @ Elsevier (PMID): 8991087; ● Search Scopus @ Elsevier (DOI): 10.1083/jcb.135.6.1741

(DOI: 10.1083/jcb.135.6.1741, PubMed: 8991087) M. Hirao, N. Sato, T. Kondo, S. Yonemura, M. Monden, Takuya Sasaki, Y. Takai, Sh. Tsukita and Sa. Tsukita :
Regulation mechanism of ERM (Ezrin/Radixin/Moesin) protein/plasma membrane association Possible involvement of phosphatidylinositol turnover and Rho-dependent signaling pathway.,
The Journal of Cell Biology, Vol.135, No.1, 37-51, 1996.

(要約): The ERM proteins, ezrin, radixin, and moesin, are involved in the actin filament/plasma membrane interaction as cross-linkers. CD44 has been identified as one of the major membrane binding partners for ERM proteins. To examine the CD44/ERM protein interaction in vitro, we produced mouse ezrin, radixin, moesin, and the glutathione-S-transferase (GST)/CD44 cytoplasmic domain fusion protein (GST-CD44cyt) by means of recombinant baculovirus infection, and constructed an in vitro assay for the binding between ERM proteins and the cytoplasmic domain of CD44. In this system, ERM proteins bound to GST-CD44cyt with high affinity (Kd of moesin was 9.3 +/- 1.6nM) at a low ionic strength, but with low affinity at a physiological ionic strength. However, in the presence of phosphoinositides (phosphatidylinositol [PI], phosphatidylinositol 4-monophosphate [4-PIP], and phosphatidylinositol 4.5-bisphosphate [4,5-PIP2]), ERM proteins bound with a relatively high affinity to GST-CD44cyt even at a physiological ionic strength: 4,5-PIP2 showed a marked effect (Kd of moesin in the presence of 4,5-PIP2 was 9.3 +/- 4.8 nM). Next, to examine the regulation mechanism of CD44/ERM interaction in vivo, we reexamined the immunoprecipitated CD44/ERM complex from BHK cells and found that it contains Rho-GDP dissociation inhibitor (GDI), a regulator of Rho GTPase. We then evaluated the involvement of Rho in the regulation of the CD44/ERM complex formation. When recombinant ERM proteins were added and incubated with lysates of cultured BHK cells followed by centrifugation, a portion of the recombinant ERM proteins was recovered in the insoluble fraction. This binding was enhanced by GTP gamma S and markedly suppressed by C3 toxin, a specific inhibitor of Rho, indicating that the GTP form of Rho in the lysate is required for this binding. A mAb specific for the cytoplasmic domain of CD44 also markedly suppressed this binding, identifying most of the binding partners for exogenous ERM proteins in the insoluble fraction as CD44. Consistent with this binding analysis, in living BHK cells treated with C3 toxin, most insoluble ERM proteins moved to soluble compartments in the cytoplasm, leaving CD44 free from ERM. These findings indicate that Rho regulates the CD44/ERM complex formation in vivo and that the phosphatidylinositol turnover may be involved in this regulation mechanism.
(キーワード): ADP Ribose Transferases / Animals / Antibodies, Monoclonal / Antigens, CD44 / Binding, Competitive / Blood Proteins / Botulinum Toxins / Cell Line / Cell Membrane / Cricetinae / Cytoplasm / Cytoskeletal Proteins / GTP-Binding Proteins / Glutathione Transferase / Guanine Nucleotide Dissociation Inhibitors / Guanosine 5'-O-(3-Thiotriphosphate) / Kidney / Membrane Proteins / Mice / Microfilament Proteins / Phosphatidylinositol 4,5-Diphosphate / Phospholipids / Phosphoproteins / Protein Binding / Proteins / Recombinant Fusion Proteins / Signal Transduction / rho-Specific Guanine Nucleotide Dissociation Inhibitors / rhoB GTP-Binding Protein
(出版サイトへのリンク): ● Publication site (DOI): 10.1083/jcb.135.1.37
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 8858161; ● Search Scopus @ Elsevier (PMID): 8858161; ● Search Scopus @ Elsevier (DOI): 10.1083/jcb.135.1.37

(DOI: 10.1083/jcb.135.1.37, PubMed: 8858161) Ryutaro Komuro, Takuya Sasaki, Kenji Takaishi, Satoshi Orita and Yoshimi Takai :
Involvement of Rho and Rac small G proteins and Rho GDI in Ca²⁺-dependent exocytosis from PC12 cells.,
Genes to Cells, Vol.1, No.10, 943-951, 1996.

(要約): The Rho small G protein family, which includes the Rho, Rac and Cdc42 subfamilies, is implicated in various cell functions such as cell shape change, cell motility and cytokinesis, through the reorganization of actin filaments. Rho GDI is an inhibitory regulator of the Rho small G protein family and inhibits the Rho family dependent cell functions. Reorganization of actin filaments is also known to regulate Ca2+-dependent exocytosis. We have examined here whether the Rho family members are also involved in Ca2+-dependent exocytosis. We have found, by the use of the human growth hormone (GH) co-expression assay system on PC12 cells, that overexpression of Rho GDI inhibits high K+-induced, Ca2+-dependent GH release. This inhibitory action of Rho GDI is restored by co-expression of a dominant active mutant of RhoA or Rac1, but not of a dominant active mutant of Cdc42. C3 transferase, known to ADP-ribosylate Rho and to inhibit its function, also inhibits this GH release. Overexpression of a dominant active mutant of RhoA or Rac1 alone shows only a small effect on GH release. Moreover, immunocytochemical studies show that the overexpression of Rho GDI prevents a partial disruption of the cortical actin network which accompanies exocytosis. These results suggest that RhoA, Rac1 and Rho GDI are involved in Ca2+-dependent exocytosis at least partly through the reorganization of actin filaments, and that the activation of RhoA or Rac1 alone is not sufficient for this reaction.
(キーワード): ADP Ribose Transferases / Actin Cytoskeleton / Actins / Animals / Botulinum Toxins / カルシウム (calcium) / Cell Cycle Proteins / Exocytosis / GTP-Binding Proteins / Growth Hormone / Guanine Nucleotide Dissociation Inhibitors / Mutation / PC12 Cells / カリウム (potassium) / Rats / Recombinant Proteins / cdc42 GTP-Binding Protein / rac GTP-Binding Proteins / rho GTP-Binding Proteins / rhoA GTP-Binding Protein
(出版サイトへのリンク): ● Publication site (DOI): 10.1046/j.1365-2443.1996.760276.x
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 9077452; ● Search Scopus @ Elsevier (PMID): 9077452; ● Search Scopus @ Elsevier (DOI): 10.1046/j.1365-2443.1996.760276.x

(DOI: 10.1046/j.1365-2443.1996.760276.x, PubMed: 9077452) Y. Takai, Takuya Sasaki, H. Shirataki and H. Nakanishi :
Rab3A small GTP-binding protein in Ca²⁺ -dependent exocytosis.,
Genes to Cells, Vol.1, No.7, 615-632, 1996.

(要約): There exists a small GTP-binding protein (G protein) superfamily, consisting of more than 50 members, from yeast to mammal. The Rab family belongs to this superfamily and is implicated in intracellular vesicle trafficking. Rab3A small G protein is a member of the Rab3 subfamily which belongs to this Rab family. The regulators and downstream targets of Rab3A have been isolated, and evidence is accumulating that Rab3A and these Rab3A-interacting proteins are involved in Ca(2+)-dependent exocytosis, particularly in neurotransmitter release from nerve terminals.
(キーワード): Amino Acid Sequence / Animals / Calcium / Exocytosis / GTP-Binding Proteins / Guanine Nucleotide Dissociation Inhibitors / Humans / Molecular Structure / Neurotransmitter Agents / Subcellular Fractions / Synaptic Vesicles / Tissue Distribution / rab3 GTP-Binding Proteins
(出版サイトへのリンク): ● Publication site (DOI): 10.1046/j.1365-2443.1996.00257.x
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 9078389; ● Search Scopus @ Elsevier (PMID): 9078389; ● Search Scopus @ Elsevier (DOI): 10.1046/j.1365-2443.1996.00257.x

(DOI: 10.1046/j.1365-2443.1996.00257.x, PubMed: 9078389) Satoshi Orita, Takuya Sasaki, R Komuro, G. Sakaguchi and M Maeda :
Doc2 enhances Ca²⁺-dependent exocytosis from PC12 cells.,
The Journal of Biological Chemistry, Vol.271, No.13, 7257-7260, 1996.

(要約): We previously isolated a new protein having two C2-like domains which interacted with Ca2+ and phospholipid and named Doc2 (Double C2). Because Doc2 was abundantly expressed in brain where it was highly concentrated on the synaptic vesicle fraction, we have examined here whether Doc2 is involved in Ca2+-dependent exocytosis from cultured PC12 cells. For this purpose, we took advantage of the growth hormone (GH) co-expression assay system of PC12 cells in which GH is stored in dense core vesicles and released in response to high K+ in an extracellular Ca2+-dependent manner. Northern and Western blot analyses indicated that Doc2 is present in PC12 cells. Overexpression of hemagglutinin-tagged Doc2 stimulated the Ca2+-dependent, high K+-induced release of co-expressed GH without affecting the basal release. In the PC12 cells transfected with a plasmid with the coding sequence of Doc2 in the antisense orientation, the high K+-induced release of co-expressed GH was inversely inhibited. The Doc2 mutant expressing an N-terminal fragment or a C-terminal fragment containing two C2-like domains inhibited the high K+-induced release of co-expressed GH. These results indicate that Doc2 enhances Ca2+-dependent exocytosis of dense core vesicles from PC12 cells.
(キーワード): Amino Acid Sequence / Animals / Blotting, Northern / Calcium / Calcium-Binding Proteins / Exocytosis / Gene Expression / Glutathione Transferase / Growth Hormone / Hemagglutinins / Kinetics / Molecular Sequence Data / Nerve Tissue Proteins / PC12 Cells / Plasmids / Potassium / Rats / Recombinant Fusion Proteins / Recombinant Proteins / Sequence Tagged Sites / Transfection
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 8631736; ● Search Scopus @ Elsevier (PMID): 8631736

(PubMed: 8631736) S. Orita, Takuya Sasaki, R. Komuro, G. Sakaguchi, M. Maeda, H. Igarashi and Y. Takai :
Doc2 enhances Ca²⁺-dependent exocytosis from PC12 cells.,
The Journal of Biological Chemistry, Vol.271, No.13, 7257-7260, 1996. Y. Fujita, Takuya Sasaki, K. Fukui, H. Kotani, T. Kimura, Y. Hata, T.C. Sdhof, R.H. Scheller and Y. Takai :
Phosphorylation of Munc-18/n-Sec1/rbSec1 by protein kinase C Its implication in regulating the interaction of Munc-18/n-Sec1/rbSec1 with Syntaxin.,
The Journal of Biological Chemistry, Vol.271, No.13, 7265-7268, 1996. T. Taniguchi, K. Takaishi, T. Murayama, M. Ito, N. Iwata, K. Chihara, Takuya Sasaki, Y. Takai and T. Matsui :
Cholecystokinin-B/gastrin receptors mediate rapid formation of actin stress fibers.,
Oncogene, Vol.12, No.6, 1357-1360, 1996. R. Komuro, Takuya Sasaki, Satoshi Orita, M. Maeda and Y. Takai :
Involvement of rabphilin-3A in Ca²⁺-dependent exocytosis from PC12 cells.,
Biochemical and Biophysical Research Communications, Vol.219, No.2, 435-440, 1996.

(要約): Rabphilin-3A, a putative target molecule of Rab3A small GTP-binding protein implicated in Ca2+-dependent exocytosis, consists of two functionally different domains: the N-terminal Rab3A-binding domain and the C-terminal two C2-like domains (C2A and C2B domains) interacting with Ca2+ and phospholipid. Here, we used the growth hormone (GH) co-expression assay system of PC12 cells in which expressed GH is released in response to high K+. Reduction of endogenous rabphilin-3A inhibited the Ca2+-dependent, high K+-induced GH release. Various rabphilin-3A mutants expressing an N-terminal, C-terminal, or C2B fragment, but not the rabphilin-3A mutant expressing a C2A fragment, inhibited the high K+-induced GH release. These results indicate that rabphilin-3A is involved at least in Ca2+-dependent exocytosis from PC12 cells and that the C2A and C2B domains have different functions.
(キーワード): Adaptor Proteins, Signal Transducing / Amino Acid Sequence / Animals / Calcium / Exocytosis / GTP-Binding Proteins / Growth Hormone / Humans / Molecular Sequence Data / Mutagenesis / Mutagenesis, Insertional / Nerve Tissue Proteins / PC12 Cells / Rats / Recombinant Fusion Proteins / Sequence Deletion / Sequence Tagged Sites / Transfection / Vesicular Transport Proteins / rab GTP-Binding Proteins
(出版サイトへのリンク): ● Publication site (DOI): 10.1006/bbrc.1996.0251
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 8605005; ● Search Scopus @ Elsevier (PMID): 8605005; ● Search Scopus @ Elsevier (DOI): 10.1006/bbrc.1996.0251

(DOI: 10.1006/bbrc.1996.0251, PubMed: 8605005) S. Matsuda, H. Nakanishi, Takuya Sasaki and Y. Takai :
A membrane-associated GDP/GTP exchange protein specific for Rho small GTP-binding protein Partial purification and characterization from rat brain.,
Oncogene, Vol.12, No.4, 915-920, 1996. R. Komuro, Takuya Sasaki, S. Orita, M. Maeda and Y. Takai :
Involvement of rabphilin-3A in Ca²⁺-dependent exocytosis from PC12 cells.,
Biochemical and Biophysical Research Communications, Vol.219, No.2, 435-440, 1996. K. Takahashi, Takuya Sasaki and Y. Takai :
Heterotetramer formation of prenylated Rab3A with two Rabphilin-3A molecules.,
Biochemical and Biophysical Research Communications, Vol.217, No.3, 979-986, 1995. H. Kuribara, K. Tago, T. Yokozeki, Takuya Sasaki, Y. Takai, N. Morii, S. Narumiya, T. Katada and Y. Kanaho :
Synergistic activation of rat brain phospholipase D by ADP-ribosylation factor and rhoA p21, and its inhibition by clostridium botulinum C3 exoenzyme.,
The Journal of Biological Chemistry, Vol.270, No.43, 25667-25671, 1995. R. Regazzi, Takuya Sasaki, K. Takahashi, J-C. Jonas, C. Volker, B. J. Stock, Y. Takai and B. C. Wollheim :
Prenylcysteine analogs mimicking the C-terminus of GTP-binding proteins stimulate exocytosis from permeabilized HIT-T15 cells comparison with the effect of Rab3AL peptide.,
Biochim. Biophys. Acta, Vol.1268, No.3, 269-278, 1995. K. Takaishi, Takuya Sasaki, T. Kameyama, Sa. Tsukita, Sh. Tsukita and Y. Takai :
Translocation of activated Rho from the cytoplasm to membrane ruffling area, cell-cell adhesion sites and cleavage furrows.,
Oncogene, Vol.11, No.1, 39-48, 1995. K. Araki, H. Nakanishi, H. Hirano, M. Kato, Takuya Sasaki and Y. Takai :
Purification and characterization of Rab GDI beta from rat brain.,
Biochemical and Biophysical Research Communications, Vol.211, No.1, 296-305, 1995. Y. Takai, Takuya Sasaki, K. Tanaka and H. Nakanishi :
Rho as a regulator of the cytoskeleton.,
Trends Biochem. Sci., Vol.20, No.6, 227-231, 1995. Satoshi Orita, Takuya Sasaki, A Naito, R Komuro and T Ohtsuka :
Doc2: a novel brain protein having two repeated C2-like domains.,
Biochemical and Biophysical Research Communications, Vol.206, No.2, 439-448, 1995.

(要約): Two repeated C2-like domains interacting with Ca2+ and phospholipid are found in synaptotagmin and Rabphilin-3A which are implicated in neurotransmitter release. Here we have isolated a cDNA encoding a novel protein having two repeated C2-like domains from a human brain cDNA library. The isolated cDNA encodes a protein with 400 amino acids and a M(r) of 44,071. The purified recombinant protein indeed interacts with Ca2+ and phospholipid. We have named this protein Doc2 (Double C2). Doc2 is exclusively expressed in brain and is highly concentrated in the synaptic vesicle fraction. These results suggest that Doc2 is a novel brain protein and serves as a Ca2+ sensor in neurotransmitter release.
(キーワード): Adaptor Proteins, Signal Transducing / Amino Acid Sequence / Base Sequence / Blotting, Northern / Blotting, Western / Brain / Calcium / Calcium-Binding Proteins / Cloning, Molecular / DNA, Complementary / Escherichia coli / GTP-Binding Proteins / Gene Library / Humans / Membrane Glycoproteins / Molecular Sequence Data / Molecular Weight / Nerve Tissue Proteins / Oligodeoxyribonucleotides / Organ Specificity / Phospholipids / Polymerase Chain Reaction / RNA, Messenger / Recombinant Fusion Proteins / Recombinant Proteins / Repetitive Sequences, Nucleic Acid / Sequence Homology, Amino Acid / Synaptic Vesicles / Synaptotagmins / Vesicular Transport Proteins / rab GTP-Binding Proteins
(出版サイトへのリンク): ● Publication site (DOI): 10.1006/bbrc.1995.1062
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 7826360; ● Search Scopus @ Elsevier (PMID): 7826360; ● Search Scopus @ Elsevier (DOI): 10.1006/bbrc.1995.1062

(DOI: 10.1006/bbrc.1995.1062, PubMed: 7826360) S. Orita, Takuya Sasaki, A. Naito, R. Komuro, T. Ohtsuka, M. Maeda, H. Suzuki, H. Igarashi and Y. Takai :
Doc2: a novel brain protein having two repeated C2-like domains.,
Biochemical and Biophysical Research Communications, Vol.206, No.2, 439-448, 1995. Y. Takai, K. Kaibuchi, A. Kikuchi and Takuya Sasaki :
Effects of prenyl modifications on interactions of small G proteins with regulators.,
Methods in Enzymology, Vol.250, 122-133, 1995. K. Tanaka, Takuya Sasaki and Y. Takai :
Purification and properties of recombinant Rho-GDP dissociation inhibitor.,
Methods in Enzymology, Vol.256, 41-49, 1995. K. Takaishi, Takuya Sasaki and Y. Takai :
Cell motility assay and inhibition by Rho-GDP dissociation inhibitor.,
Methods in Enzymology, Vol.256, 336-347, 1995. Takuya Sasaki and Y. Takai :
Purification and Properties of bovine Rab-GDP dissociation inhibitor.,
Methods in Enzymology, Vol.257, 70-79, 1995. M. Kato, Takuya Sasaki, K. Imazumi, K. Takahashi, K. Araki, H. Shirataki, Y. Matsuura, A. Ishida, H. Fujisawa and Y. Takai :
Phosphorylation of Rabphilin-3A by calmodulin-dependent protein kinase II.,
Biochemical and Biophysical Research Communications, Vol.205, No.3, 1776-1784, 1994. K. Imazumi, Takuya Sasaki, K. Takahashi and Y. Takai :
Identification of a Rabphilin-3A-interacting protein as GTP cyclohydorase I in PC12 cells.,
Biochemical and Biophysical Research Communications, Vol.205, No.2, 1409-1416, 1994. Y. Fujita, Takuya Sasaki, K. Araki, K. Takahashi, K. Imazumi, M. Kato, Y. Matsuura and Y. Takai :
GDP/GTP exchange reaction-stimulating activity of Rabphilin-3A for Rab3A small GTP-binding protein.,
FEBS Letters, Vol.353, No.1, 67-70, 1994. A. Miyazaki, Takuya Sasaki, K. Araki, N. Ueno, K. Imazumi, Fumiko Nagano, K. Takahashi and Y. Takai :
Comparison of kinetic properties between MSS4 and Rab3A GRF GDP/GTP exchange proteins.,
FEBS Letters, Vol.350, No.2-3, 333-336, 1994. A. Mizoguchi, Y. Yano, H. Hamaguchi, H. Yanagida, C. Ide, A. Zahraoui, H. Shirataki, Takuya Sasaki and Y. Takai :
Localization of Rabphilin-3A on the synaptic vesicle.,
Biochemical and Biophysical Research Communications, Vol.202, No.3, 1235-1243, 1994. Takayuki Nishiyama, Takuya Sasaki, Kenji Takaishi, Masaki Kato, Hideaki Yaku, Keishi Araki, Yoshiharu Matsuura and Yoshimi Takai :
rac p21 is involved in insulin-induced membrane ruffling and rho p21 is involved in hepatocyte growth factor- and 12-O-tetradecanoylphorbol-13-acetate(TPA)-induced membrane ruffling in KB cells.,
Molecular and Cellular Biology, Vol.14, No.4, 2447-2456, 1994. H. Yaku, Takuya Sasaki and Y. Takai :
The Dbl oncogene product as a GDP/GTP exchange protein for the Rho family its properties in comparison with those of Smg GDS.,
Biochemical and Biophysical Research Communications, Vol.198, No.2, 811-817, 1994. K. Takaishi, Takuya Sasaki, M. Kato, W. Yamochi, S. Kuroda, T. Nakamura, M. Takeichi and Y. Takai :
Involvement of Rho p21 small GTP-binding protein and its regulator in the HGF-induced cell motility.,
Oncogene, Vol.9, No.1, 273-279, 1994. Takuya Sasaki, Masaki Kato and Yoshimi Takai :
Consequences of weak interaction of rho GDI with the GTP-bound forms of rho p21 and rac p21.,
The Journal of Biological Chemistry, Vol.268, No.32, 23959-23963, 1993. Shosei Kishida, Hiromichi Shirataki, Takuya Sasaki, Masaki Kato, Kozo Kaibuchi and Yoshimi Takai :
Rab3A GTPase-activating protein-inhibiting activity of Rabphilin-3A, a putative Rab3A target protein.,
The Journal of Biological Chemistry, Vol.268, No.30, 22259-22261, 1993. Michelle D. Garrett, Alisa K. Kabcenell, Joseph E. Zahner, Kozo Kaibuchi, Takuya Sasaki, Yoshimi Takai, Clarissa M. Cheney and Peter J. Novick :
Interaction of Sec4 with GDI proteins from bovine brain, drosophila melanogaster and saccharomyces cerevisiae: conservation of GDI membrane dissociation activity.,
FEBS Letters, Vol.331, No.3, 233-238, 1993. Tohru Sawai, Makoto Asada, Hiroyuki Nunoi, Ichiro Matsuda, Satoshi Ando, Takuya Sasaki, Kozo Kaibuchi, Yoshimi Takai and Kouichi Katayama :
Combination of arachidonic acid and guanosine 5-O-(3-thiotriphosphate) induce translocation of rac p21s to membrane and activation of NADPH oxidase in a cell-free system.,
Biochemical and Biophysical Research Communications, Vol.195, No.1, 264-269, 1993. Oliver Ullrich, Harald Stenmark, Kirill Alexandrov, Lukas A. Huber, Kozo Kaibuchi, Takuya Sasaki, Yoshimi Takai and Marino Zerial :
Rab GDP dissociation inhibitor as a general regulator for the membrane association of rab proteins.,
The Journal of Biological Chemistry, Vol.268, No.24, 18143-18150, 1993. Takuya Sasaki, Masaki Kato, Takayuki Nishiyama and Yoshimi Takai :
The nucleotide exchange rates of Rho and Rac small GTP-binding proteins are enhanced to different extents by their regulatory protein Smg GDS.,
Biochemical and Biophysical Research Communications, Vol.194, No.3, 1188-1193, 1993. Kiyohiko Kishi, Takuya Sasaki, Shinya Kuroda, Takahito Itoh and Yoshimi Takai :
Regulation of cytoplasmic division of Xenopus embryo by rho p21 and its inhibitory GDP/GTP exchange protein (rho GDI).,
The Journal of Cell Biology, Vol.120, No.5, 1187-1195, 1993.

(要約): Evidence is accumulating that the rho family, a member of the ras p21-related small GTP-binding protein superfamily, regulates cell morphology, cell motility, and smooth muscle contraction through the actomyosin system. The actomyosin system is also known to be essential for cytoplasmic division of cells (cytokinesis). In this study, we examined the action of rho p21, its inhibitory GDP/GTP exchange protein, named rho GDI, its stimulatory GDP/GTP exchange protein, named smg GDS, and botulinum ADP-ribosyltransferase C3, known to selectively ADP-ribosylate rho p21 and to impair its function, in the cytoplasmic division using Xenopus embryos. The sperm-induced cytoplasmic division of Xenopus embryos was not affected by microinjection into the embryos of either smg GDS or the guanosine-5'-(3-O-thio)triphosphate (GTP gamma S)-bound form of rhoA p21, one member of the rho family, but completely inhibited by microinjection of rho GDI or C3. Under these conditions, nuclear division occurred normally but the furrow formation, which was induced by the contractile ring consisting of actomyosin just beneath the plasma membrane, was impaired. Comicroinjection of rho GDI with the GTP gamma S-bound form of rhoA p21 prevented the rho GDI action. Moreover, the sperm-induced cytoplasmic division of Xenopus embryos was inhibited by microinjection into the embryos of the rhoA p21 pre-ADP-ribosylated by C3 which might serve as a dominant negative inhibitor of endogenous rho p21. These results indicate that rho p21 together with its regulatory proteins regulates the cytoplasmic division through the actomyosin system.
(キーワード): ADP Ribose Transferases / Actin Cytoskeleton / Animals / Botulinum Toxins / 細胞分裂 (cell division) / Cleavage Stage, Ovum / GTP-Binding Proteins / Guanine Nucleotide Dissociation Inhibitors / Microinjections / Protein Processing, Post-Translational / 構造活性相関 (structureactivity relationship) / アフリカツメガエル (Xenopus laevis) / rab3 GTP-Binding Proteins / rho-Specific Guanine Nucleotide Dissociation Inhibitors / rhoA GTP-Binding Protein
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 8436590; ● Summary page in Scopus @ Elsevier: 2-s2.0-0027509362

(PubMed: 8436590, Elsevier: Scopus) Yasushi Miura, Akira Kikuchi, Takashi Musha, Shinya Kuroda, Hideaki Yaku, Takuya Sasaki and Yoshimi Takai :
Regulation of morphology by rho p21 and its inhibitory GDP/GTP exchange protein (rho GDI) in Swiss 3T3 cells.,
The Journal of Biological Chemistry, Vol.268, No.1, 510-515, 1993. Kenji Takaishi, Akira Kikuchi, Shinya Kuroda, Kei Kotani, Takuya Sasaki and Yoshimi Takai :
Involvement of rho p21 and its inhibitory GDP/GTP exchange protein (rho GDI) in cell motility.,
Molecular and Cellular Biology, Vol.13, No.1, 72-79, 1993. Satoshi Ando, Kozo Kaibuchi, Takuya Sasaki, Kunihiko Hiraoka, Takayuki Nishiyama, Takakazu Mizuno, Makoto Asada, Hiroyuki Nunoi, Ichiro Matsuda, Yoshiharu Matsuura, Paul Polakis, Frank McCormick and Yoshimi Takai :
Post-translational processing of rac p21s is important both for their interaction with the GDP/GTP exchange proteins and for their activation of NADPH oxidase.,
The Journal of Biological Chemistry, Vol.267, No.36, 25709-25713, 1992. Yasuhisa Yoshida, Masahito Kawata, Yasushi Miura, Takashi Musha, Takuya Sasaki, Akira Kikuchi and Yoshimi Takai :
Microinjection of smg/rap1/Krev-1 p21 into Swiss 3T3 cells induces DNA synthesis and morphological changes.,
Molecular and Cellular Biology, Vol.12, No.8, 3407-3414, 1992. Akira Kikuchi, Shinya Kuroda, Takuya Sasaki, Kei Kotani, Ken-ichi Hirata, Masaya Katayama and Yoshimi Takai :
Functional interactions of stimulatory and inhibitory GDP/GTP exchange proteins and their common substrate small GTP-binding protein.,
The Journal of Biological Chemistry, Vol.267, No.21, 14611-14615, 1992. Shinya Kuroda, Akira Kikuchi, K. Hirata, T. Masuda, K. Kishi, Takuya Sasaki and Yoshimi Takai :
Cooperative function of rho GDS and rho GDI to regulate rho p21 activation in smooth muscle.,
Biochemical and Biophysical Research Communications, Vol.185, No.1, 473-480, 1992. Ken-ichi Hirata, Akira Kikuchi, Takuya Sasaki, Shinya Kuroda, Kozo Kaibuchi, Yoshiharu Matsuura, Hitomi Seki and Kooichi Saida :
Involvement of rho p21 in the GTP-enhanced calcium ion sensitivity of smooth muscle contraction.,
The Journal of Biological Chemistry, Vol.267, No.13, 8719-8722, 1992. Hiromichi Shirataki, Kozo Kaibuchi, Motoki Hiroyoshi, Mitsuo Isomura, Shin Araki, Takuya Sasaki and Yoshimi Takai :
Inhibition of the action of the stimulatory GDP/GTP exchange protein for smg p21 by the geranylgeranylated synthetic peptides designed from its C-terminal region.,
The Journal of Biological Chemistry, Vol.266, No.31, 20672-20677, 1991. Takahito Itoh, Kozo Kaibuchi, Takuya Sasaki and Yoshimi Takai :
The smg GDS-induced activation of smg p21 is initiated by cyclic AMP-dependent protein kinase-catalyzed phosphorylation of smg p21.,
Biochemical and Biophysical Research Communications, Vol.177, No.3, 1319-1324, 1991. Takuya Sasaki :
A novel type of regulatory protein for the GDP/GTP exchange reaction of smg p25A, a ras p21-like small GTP-binding protein, in bovine brain cytosol.,
Kobe J. Med. Sci., Vol.37, No.3, 129-145, 1991. Yutaka Hata, Akira Kikuchi, Takuya Sasaki, Michael D. Schaber and Jackson B. Gibbs :
Inhibition of the ras p21 GTPase-activating protein-stimulated GTPase activity of c-Ha-ras p21 by smg p21 having the same putative effector domain as ras p21s.,
The Journal of Biological Chemistry, Vol.265, No.13, 7104-7107, 1991. Takuya Sasaki, Kozo Kaibuchi, Alisa K. Kabcenell, Peter J. Novick and Yoshimi Takai :
A mammalian inhibitory GDP/GTP exchange protein (GDP dissociation inhibitor) for smg p25A is active on the yeast SEC4 protein.,
Molecular and Cellular Biology, Vol.11, No.5, 2909-2912, 1991. Shin Araki, Kozo Kaibuchi, Takuya Sasaki, Yutaka Hata and Yoshimi Takai :
Role of the C-terminal region of smg p25A in its interaction with membranes and the GDP/GTP exchange protein.,
Molecular and Cellular Biology, Vol.11, No.3, 1438-1447, 1991. Takuya Sasaki, Akira Kikuchi, Shin Araki, Yutaka Hata, Mitsuo Isomura, Shinya Kuroda and Yoshimi Takai :
Purification and characterization from bovine brain cytosol of a protein that inhibits the dissociation of GDP from and the subsequent binding of GTP to smg p25A, a ras p21-like GTP-binding protein.,
The Journal of Biological Chemistry, Vol.265, No.4, 2333-2337, 1990. Akira Kikuchi, Takuya Sasaki, Shin Araki, Yutaka Hata and Yoshimi Takai :
Purification and characterization from bovine brain cytosol of two GTPase- activating proteins specific for smg p21, a GTP-binding protein having the same effector domain as c-ras p21s.,
The Journal of Biological Chemistry, Vol.264, No.16, 9133-9136, 1989.

MISC

研究者総覧に該当データはありませんでした。

総説・解説

坂根亜由子, 佐々木卓也 :
Rab3Aと神経可塑性,
生体の科学, Vol.61, No.5, 426-427, 2010年. 佐々木卓也 :
ものの重み，努力の重み，人の重み,
細胞工学, Vol.28, No.12, 1269-1270, 2009年11月. 佐々木卓也 :
基礎の基礎,
細胞工学, Vol.28, No.12, 1218-1221, 2009年11月. 坂根亜由子, 佐々木卓也 :
RabファミリーSmall Gタンパク質による小胞輸送制御と高次生命機能,
細胞工学, Vol.28, No.12, 1247-1252, 2009年11月.

(キーワード): Rab / 小胞輸送 / 活性制御タンパク質 / 標的タンパク質
(文献検索サイトへのリンク): ● CiNii @ 国立情報学研究所 (CRID): 1520291855510311808

(CiNii: 1520291855510311808) 坂根亜由子, 佐々木卓也 :
高次機能システムを支えるエキソサイトーシス系Rabファミリー低分子量GTPase,
蛋白質核酸酵素, Vol.53, No.16, 2130-2135, 2008年12月.

(キーワード): 高次機能システム / 調節性エキソサイトーシス / Rabファミリー低分子量GTPase
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 21038597; ● CiNii @ 国立情報学研究所 (CRID): 1523669554608441216; ● Search Scopus @ Elsevier (PMID): 21038597

(PubMed: 21038597, CiNii: 1523669554608441216) 坂根亜由子, 佐々木卓也 :
シナプス伝達と可塑性を支える小胞輸送 —Rab3A系を中心とした神経伝達物質放出の制御機構—,
実験医学, Vol.24, No.14, 2098-2103, 2006年9月. 坂根亜由子, 佐々木卓也 :
神経可塑性とRab3A,
Clinical Neuroscience, Vol.24, No.7, 826, 2006年7月. 西村範行, 東尾浩典, 佐々木卓也 :
接着分子のリサイクリング,
生体の科学, Vol.57, No.2, 128-133, 2006年4月. 坂根亜由子, 佐々木卓也 :
神経伝達物質放出の制御機構—開口分泌を制御するRab低分子量G蛋白質に注目して,
内分泌・糖尿病科, Vol.25, No.3, 200-205, 2006年. 坂根亜由子, 佐々木卓也 :
神経伝達物質放出の制御分子群とCa2+チャネル,
医学のあゆみ別冊イオンチャネル最前線update 臓器でのイオンチャネルの働きと疾患, 197-202, 2005年8月. 西村範行, 佐々木卓也 :
細胞内小胞輸送のしくみ,
G. I. Research, Vol.12, No.3, 242-248, 2004年6月. 佐々木卓也, 西村範行, 水野広一, 真鍋進治 :
徳島発の臨床応用を目指した基礎研究—トランスレーショナルリサーチを視野に入れた「小胞輸送」の研究—,
四国医学雑誌, Vol.59, No.1-2, 2-6, 2003年4月.

(徳島大学機関リポジトリ): ● Metadata: 110576

(徳島大学機関リポジトリ: 110576) 佐々木卓也, 西村範行, 水野広一 :
Rabファミリー低分子量Gタンパク質による細胞内小胞輸送制御,
わかる実験医学シリーズ:細胞内輸送がわかる(米田悦啓編), 111-115, 2002年10月. 佐々木卓也 :
神経伝達物質放出の制御分子群とCa²⁺チャンネル,
医学のあゆみ, Vol.201, No.13, 1107-1112, 2002年6月. 佐々木卓也, 織田聡, 三好淳, 高井義美 :
神経伝達物質放出の調節機構と高次神経機能,
脳の科学, Vol.23, No.4, 297-306, 2001年4月. 萬本明子, 佐々木卓也, 高井義美 :
Rhoファミリーによるアクチン細胞骨格系の時間的, 空間的制御,
がん遺伝子・がん抑制遺伝子(渋谷正史, 山本雅編), 87-94, 1999年9月. 織田聡, 佐々木卓也, 高井義美 :
Doc2を介する神経伝達物質放出のメカニズム.,
生化学, Vol.71, No.7, 530-535, 1999年7月.

(文献検索サイトへのリンク): ● CiNii @ 国立情報学研究所 (CRID): 1520009410498934144

(CiNii: 1520009410498934144) 永野史子, 佐々木卓也, 高井義美 :
シナプス伝達,
細胞内物質輸送のダイナミズム(米田悦啓, 中野明彦編), 151-160, 1999年. 織田聡, 佐々木卓也, 高井義美 :
Doc2を介する神経伝達物質放出と記憶形成のメカニズム.,
実験医学, Vol.16, 1554-1560, 1998年. 織田聡, 佐々木卓也, 高井義美 :
Doc2を介する神経伝達物質の放出と記憶形成のメカニズム,
実験医学増刊, Vol.16, 1554-1560, 1998年. 佐々木卓也 :
dbl,
Bio Science用語ライブラリー「癌遺伝子・癌抑制遺伝子」(田矢洋一, 山本雅編), 58-59, 1997年10月. 織田聡, 佐々木卓也, 阪口岳, 高井義美 :
C2領域を2つ有する一群のタンパク質と神経伝達物質の放出機構.,
実験医学, Vol.15, 1619-1627, 1997年. 徳永正浩, 佐々木卓也, 高井義美 :
Rab3Aと神経伝達物質の放出機構,
神経精神薬理 200号記念増刊号, 36-44, 1997年. 織田聡, 佐々木卓也, 阪口岳, 高井義美 :
C2領域を2つ有する一群のタンパク質と神経伝達物質の放出機構,
実験医学増刊, Vol.15, 1619-1627, 1997年. 佐々木卓也, 高井義美 :
分泌のメカニズムとG蛋白質,
最新内科学大系内科総論2 科学としての内科学(井村裕夫, 尾形悦郎, 高久史麿, 垂井清一郎編), 171-180, 1996年11月. 朝倉剛, 佐々木卓也, 高井義美 :
低分子量GTP結合蛋白質,
免疫研究法ハンドブック改訂2版(藤原大美, 淀井敦司編), 393-408, 1996年11月. 佐々木卓也, 田中一馬, 白瀧博通, 高井義美 :
低分子量G蛋白質,
シグナル伝達と病態 — 阿蘇シンポジウム1995 —(高月清, 尾上薫編), 1-15, 1996年7月. 田中一馬, 佐々木卓也, 白瀧博通, 高井義美 :
低分子量Gタンパク質,
別冊日経サイエンス, Vol.116, 82-91, 1996年6月. 荒木敬司, 佐々木卓也 :
低分子量GTP結合蛋白質の解析法,
バイオマニュアルUPシリーズシグナル伝達実験法(宇井理生編), 108-123, 1996年3月. 織田聡, 佐々木卓也 :
Doc2.,
実験医学, Vol.14, 347-349, 1996年. 高石健司, 佐々木卓也 :
Rhoと細胞運動,
実験医学増刊, Vol.14, 301-303, 1996年. 高橋和男, 高石健司, 佐々木卓也 :
RhoとERMファミリー,
実験医学増刊, Vol.14, 309-311, 1996年. 佐々木卓也, 高井義美 :
Rabの機能と作用機構,
実験医学増刊, Vol.14, 327-329, 1996年. 平野尚伸, 佐々木卓也, 中西宏之 :
RabのGEPとGAP,
実験医学増刊, Vol.14, 332-334, 1996年. 加藤正樹, 佐々木卓也 :
Rab GDIの機能と作用機構,
実験医学増刊, Vol.14, 335-337, 1996年. 織田聡, 佐々木卓也 :
Doc2,
実験医学増刊, Vol.14, 347-349, 1996年. 松田修二, 佐々木卓也, 高井義美 :
Rasシグナルカスケード,
新臨床医のための分子医学シリーズ「細胞内情報伝達のしくみ」(宇井理生編), 85-102, 1996年. 佐々木卓也 :
Dbl,
Bio Science用語ライブラリー「細胞内シグナル伝達」(山本雅編), 92-93, 1995年9月. 佐々木卓也 :
Cdc25/Ras GRF,
Bio Science用語ライブラリー「細胞内シグナル伝達」(山本雅編), 96-97, 1995年9月. 今住克則, 佐々木卓也, 高井義美 :
RabとRho低分子量G蛋白質のシグナル伝達系における分子間相互作用,
実験医学増刊, Vol.13, 646-656, 1995年. 高石健司, 佐々木卓也, 高井義美 :
Rho低分子量G蛋白質による接着分子の制御,
実験医学, Vol.13, 2162-2167, 1995年. 織田聡, 佐々木卓也, 高井義美 :
低分子量GTP結合蛋白質の機能と活性制御「RasとRhoの機能と作用機構」,
最新医学からのアプローチ「GTP結合蛋白質」(宇井理生編), Vol.11, 92-111, 1994年6月. Y. Takai, K. Kaibuchi, Takuya Sasaki, H. Shirataki, K. Tanaka and H. Nakanishi :
The regulatory and target proteins for small G proteins.,
GTPase-Controlled Molecular Machines (Corda, D., Hamm, H., and Luini A., eds.), 221-233, 1994. 宮崎睦雄, 佐々木卓也, 高井義美 :
Rab 3A, Rabphilin 3Aと神経伝達物質の放出機構,
細胞工学, Vol.13, 367-371, 1994年. 西山隆之, 佐々木卓也, 高井義美 :
Rhoによる細胞骨格制御,
実験医学増刊, Vol.12, 991-996, 1994年. 高石健司, 佐々木卓也, 高井義美 :
Rhoによる細胞運動・細胞接着の制御,
医学のあゆみ, Vol.171, 331-336, 1994年. 夜久英明, 黒田真也, 佐々木卓也 :
血管平滑筋における低分子量GTP結合タンパク質の機能,
Molecular Medicine, Vol.30, 354-362, 1993年. 黒田真也, 佐々木卓也 :
rho p21の標的としての細胞骨格をめぐるトピックス,
実験医学, Vol.11, 471-475, 1993年. 安藤賢, 佐々木卓也, 高井義美 :
低分子量G蛋白質の機能と作用機構,
実験医学増刊, Vol.11, 79-86, 1993年. 高井義美, 貝淵弘三, 佐々木卓也, 田中一馬, 白瀧博通 :
Rasスーパーファミリー — RasとRhoの機能, 活性化機構および作用機構,
[最新医学・48巻・増刊号「癌解明への新しいアプローチ — 臨床遺伝子学'93」(豊島久真男, 他編)], 120-139, 1993年. 平田健一, 佐々木卓也 :
平滑筋収縮と低分子量Gタンパク質,
細胞工学, Vol.11, 414-419, 1992年. 高石健司, 佐々木卓也, 高井義美 :
低分子量GTP結合蛋白質の解析法,
実験医学, Vol.11, 238-244, 1992年. Yoshimi Takai, Kozo Kaibuchi, Akira Kikuchi, M. Kawata, Takuya Sasaki and Y Kawahara :
Possible functions and mode of action of smg p21 in signal transduction.,
Molecular Biology of the Myocardium (Tada, M., ed.), 15-26, 1992. Yoshimi Takai, Kozo Kaibuchi, Akira Kikuchi, M. Kawata, Takuya Sasaki and T. Yamamoto :
Transforming and c-fos promotor/enhancer-stimulating activities of a GDP/GTP exchange protein for small GTP-binding proteins.,
Proceedings of the 22nd International Symposium of the Princess Takamatsu Cancer Research Fund., Multistage Carcinogenesis (Harris, C.C., Hirohashi, S., Ito, N., Pitot, H.C., Sugimura, T., Terada, M., and Yokota, J., eds.), 197-204, 1992. 佐々木卓也, 菊池章 :
GDP解離抑制蛋白質(GDI),
実験医学増刊, Vol.8, 1876-1880, 1990年.

講演・発表

Shogo Miyamura, Ryo Oe, Takuya Nakahara, Shota Okada, Shuji Taue, Yu Tokizane, Takeo Minamikawa, Taka-aki Yano, Kunihiro Otsuka, Ayuko Sakane, Takuya Sasaki, Koji Yasutomo, Taira Kajisa and Takeshi Yasui :
Rapid detection of SARS- CoV-2 nucleocapsid protein antigen by dual- comb biosensing,
SPIE Biomedical Imaging and Sensing Conference 2022 (BISC2022), 250308, Taipei, Dec. 2022. MIYAMURA Shogo, Ryo Oe, Takuya Nakahara, Shota Okada, Taira Kajisa, Shuji Taue, Yu Tokizane, Takeo Minamikawa, Taka-aki Yano, Kunihiro Otsuka, Ayuko Sakane, Takuya Sasaki, Koji Yasutomo and Takeshi Yasui :
Dual-Comb Biosensing for Rapid Detection of SARS-CoV-2,
Conference on Lasers and Electro-Optics 2022 (CLEO2022), JTh6A.6, San Jose, May 2022.

(文献検索サイトへのリンク): ● Summary page in Scopus @ Elsevier: 2-s2.0-85139913953

(Elsevier: Scopus) Takuya Sasaki and Ayuko Sakane :
Role of Rab Small G proteins in cellular morphogenesis.,
札幌国際がんシンポジウム2010「メンブレントラフィックとがん」, Sapporo, Jun. 2010. Takuya Sasaki, Noriyuki Nishimura and Ayuko Sakane :
Functions of Rab family small G proteins in regulated exocytosis.,
International Symposium on Membrane Traffic, Awaji, Nov. 2007. Nakanishi Hiroyuki, Takuya Sasaki, Miyoshi Jun and Takai Yoshimi :
Rab3A small G protein and its regulators in neurotransmitter release and synaptic plasticity,
9th International Catecholamine Symposium, Kyoto, Apr. 2001. Nakaanishi Hiroyuki, Takuya Sasaki and Takai Yoshimi :
Rab3 small G protein in neurotransmitter release.,
11th International Congress of Endocrinoligy (ICE 2000), Sydney, Nov. 2000. Takai Yoshimi, Takuya Sasaki and Miyoshi Jun :
Rab3 regulators in neurotransmission: Lessons from Rab GDI- and Rab3 GEP-deficient mice.,
Fondation Schlumberger pour l'Education et la Recherche, France, Apr. 2000. Takai Yoshimi, Takaishi Kenji and Takuya Sasaki :
Cooperative roles of Rho and Rab small G proteins in cell adhesion and migration.,
Keystone Symposia on The Functions of Small GTPases, Santa Fe, Mar. 1999. Takai Yoshimi, Takuya Sasaki, Shirataki Hiromichi and Orita Satoshi :
Role of Doc2 and tomosyn in synaptic vesicle exocytosis.,
Keystone Symposia on Molecular Physiology and Pathology of Membrane Traffic, Santa Fe, Jan. 1999. Fujiwara Takeshi, Tanaka Kazuma, Umikawa Masato, Takuya Sasaki and Takai Yoshimi :
Dynamic activation and action of the Rho familiy of small G proteins in regulation of the actin cytoskelton,
4th Joint Conference of The American Association for Cancer Research and The Japanese Cancer Association "Innovative Approaches to the Prevention, Diagnosis and Therapy of Cancer", Hawaii, Feb. 1998. Takai Yoshimi, Takuya Sasaki, Shirataki Hiromichi and Orita Satoshi :
Rab3 and Doc2 systems in Ca²⁺ -dependent neurotransmitter release.,
Keio University International Symposia for Life Sciences and Medicine, Japan, Dec. 1997. Takai Yoshimi, Tanaka Kazuma, Takuya Sasaki and Takaishi Kenji :
Temporal and spatial regulation of signal transduction in cell motility.,
The 2nd Korea-Japan Cancer Research Workshop 1997, Japan, Dec. 1997. Takai Yoshimi, Takuya Sasaki, Shirataki Hiromichi and Orita Satoshi :
Roles of proteins with C1 and C2 domains in intracellular vesicle trafficking.,
International Symposium "Dynamic Aspects of Lysosomal/Vacuolar System", Okazaki, Japan, Nov. 1997. Takai Yoshimi, Tanaka Kazuma, Takuya Sasaki, Takaishi Kenji and Takahashi Kazuo :
Dynamic activation and action of Rho in regulation of actin cytoskeleton.,
17th International Congress of Biochemistry and Molecular Biology, San Francisco, Aug. 1997. Takai Yoshimi, Tanaka Kazuma, Takuya Sasaki, Takaishi Kenji and Takahashi Kazuo :
Dynamic activation and action of Rho in regulation of actin cytoskeleton.,
The 17th International Symposium sponsored by Sapporo Cancer Seminar Foundation "Cytoskeleton and G proteins in the Regulation of Cancer", Japan, Jul. 1997. Takai Yoshimi, Tanaka Kazuma, Takuya Sasaki, Takaishi Kenji and Takahashi Kazuo :
Dynamic activation and action of Rho in regulation of actin cytoskeleton.,
FASEB Summer Research Conferences, Colorado, Jul. 1997. Tanaka Kazuma, Takuya Sasaki and Takai Yoshimi :
Activation and action of Rho in regulation of actin cytoskeleton.,
Keystone Symposia on Molecular & Cellular Biology "Temporal and Spatial Determinants in Signal Transduction", Colorado, Apr. 1997. Takai Yoshimi, Takuya Sasaki, Shirataki Hiromichi and Orita Satoshi :
Protein-membrane phospholipid interactions Roles of the C1 and C2 domains, diacylglycerol, and Ca²⁺.,
The 22th NIPS (SEIRIKEN) Conference "Under the membrane -signal transduction and integration-", Japan, Feb. 1997. Takai Yoshimi, Takuya Sasaki, Shirataki Hiromichi and Orita Satoshi :
Roles of proteins with C1 and C2 domains in Ca²⁺ -dependent neurotransmitter release.,
The Third Hamamatsu International Symposium on Biophotonics: Molecular Communication in Cellular Physiology, Japan, Feb. 1997. Takai Yoshimi, Tanaka Kazuma and Takuya Sasaki :
Mode of action and activation of Rho small G protein.,
Center for Signal Transduction Research (2nd Symposium) "Second Messengers and Signal Transduction", Korea, Sep. 1996. Takuya Sasaki, Shirataki Hiromichi, Nakanishi Hiroyuki and Takai Yoshimi :
Rab3 system in neurotransmitter release.,
12th FAOBMB Symposium, Tokushima, Jul. 1996. Takai Yoshimi, Takuya Sasaki, Shirataki Hiromichi, Nakanishi Hiroyuki and Orita Satoshi :
Mode of action of Rab3 system in Ca²⁺ -dependent exocytosis.,
BIO JAPAN '96, Japan, Jul. 1996. Takai Yoshimi, Takuya Sasaki, Shirataki Hiromichi, Nakanishi Hiroyuki and Orita Satoshi :
Mode of action of Rab3 system in neurotransmitter release.,
Uehara Memorial Foundation Symposium "Integrative and Moleculaar Approaches to Brain Function", Tokyo, Jun. 1996. Takai Yoshimi, Tanaka Kazuma and Takuya Sasaki :
Targets and regulators of Rho.,
Keystone Symposia on Molecular & Cellular Biology "Small GTP-binding Proteins and Growth Factor Signaling Pathways", Colorado, Jan. 1996. Takai Yoshimi, Tanaka Kazuma and Takuya Sasaki :
Target molecules for ras and rho small G proteins.,
Workshop on "G Proteins: Structural Features and their Involvement in the Regulation of Cell Growth", Madrid, Nov. 1995. Takai Yoshimi, Shirataki Hiromichi, Takuya Sasaki, Nakanishi Hiroyuki and Orita Satoshi :
Rabphilin-3A and Doc2 as Ca²⁺ sensors for neurotransmitter release.,
The 4th IBRO (International Brain Research Organaization) Meeting "Molecular Mechanisms of Neurotransmitter", Kyoto, Jul. 1995. Takai Yoshimi, Shirataki Hiromichi, Takuya Sasaki, Nakanishi Hiroyuki and Orita Satoshi :
Rab3A, Rabphilin and Rab GDI in neurotransmitter release.,
Satellite Symposium of 15th ISN Meeting "New Aspects of Molecular Neurosecretory Mechanisms", Hamamatsu, Jun. 1995. Kurihara Hideo, Yokozeki Takeaki, Takuya Sasaki, Takai Yoshimi, Morii Narito, Narumiya Syu, Katada Toshiaki and Kanaho Yasunori :
Synergistic activation of rat brain phospholipase D by ADP-ribosylation factor and rhoA p21.,
Satellite Meeting of 15th ISN "Lipid Messengers in The Nervous System", Hamamatsu, Jun. 1995. Takai Yoshimi, Takuya Sasaki and Shirataki Hiromichi :
Rab3A and Rabphilin-3A in neurotransmitter release.,
The Second IMSUT International Symposium for Biomedical Research "The Leading Edge of Neural and Developmental Sciences", Tokyo, Mar. 1995. 宮村祥吾, 麻植凌, 仲原拓弥, 岡田昇太, 田上周路, 時実悠, 南川丈夫, 矢野隆章, 大塚邦紘, 坂根亜由子, 佐々木卓也, 安友康二, 加治佐平, 安井武史 :
デュアル光コムバイオセンシングによるSARS-CoV-2/NP抗原の迅速·高感度検出,
学術講演会第43回年次大会, E06-19p-IX-01, 2023年1月. 宮村祥吾, 麻植凌, 仲原拓弥, 岡田昇太, 加治佐平, 時実悠, 南川丈夫, 矢野隆章, 田上周路, 大塚邦紘, 坂根亜由子, 佐々木卓也, 安友康二, 安井武史 :
新型コロナウイルスNタンパク抗原のデュアル光コム・バイオセンシング,
第83回応用物理学会秋季学術講演会, 21a-A200-4, 2022年9月. 仲原拓弥, 麻植凌, 加治佐平, 時実悠, 南川丈夫, 田上周路, 大塚邦紘, 坂根亜由子, 安友康二, 佐々木卓也, 安井武史 :
屈折率センシング光コムを用いたバイオセンシングに関する検討(4)~新型コロナウイルス(SARS-CoV-2)の検出~,
第82回応用物理学会秋季学術講演会予稿集, 13p-N322-7, 2021年9月. 加治佐平, 矢野隆章, 大塚邦紘, 九十九伸一, 坂根亜由子, 駒貴明, 野間口雅子, 安友康二, 佐々木卓也, 安井武史 :
SARS-CoV-2由来RNAの高感度検出に向けたプラズモニックバイオセンサ,
第68回応用物理学会春季学術講演会予稿集, 16p-Z22-13, 2021年3月. 坂根亜由子, 土屋裕子, 水口賢司, 佐々木卓也 :
多彩な細胞機能を構造生物学から解く-前説も兼ねて,
第19回日本蛋白質科学会年会・第71回日本細胞生物学会大会合同年次大会, 2019年6月. 富田陽子, 坂根亜由子, 三宅一央, 佐川幾子, 笠原二郎, 佐々木卓也 :
分子内結合が調節するJRABのLIMドメインによるアクチン細胞骨格の再編成,
第60回日本生化学会中国・四国支部例会, 2019年5月. 坂根亜由子, 吉澤信, 土屋裕子, 松井翼, 出口真次, 水口賢司, 横田秀夫, 佐々木卓也 :
集団的細胞運動において一分子構造変化が生み出す多様な運動様式とその役割,
第41回日本分子生物学会年会ワークショップ, 2018年11月. 坂根亜由子, 吉澤信, 松井翼, 土屋裕子, 水口賢司, 出口真次, 横田秀夫, 佐々木卓也 :
組織構築・修復過程において1分子構造変化が生み出す多彩な細胞移動とその意義,
第91回日本生化学会大会シンポジウム, 2018年9月. 土屋裕子, 坂根亜由子, 佐々木卓也, 水口賢司 :
異なるRabとエフェクター蛋白質JRABが導く多彩な細胞機能,
第18回日本蛋白質科学会年会, 2018年6月. 坂根亜由子, 佐々木卓也 :
一分子の構造変化による集団的細胞運動の制御,
日本機械学会第28回バイオフロンティア講演会キーノート講演, 2017年10月. Ayuko Sakane, 水口賢司, 土屋裕子 and Takuya Sasaki :
Conformational plasticity of JRAB/MICAL-L2 provides ``law and order'' in collective cell migration,
第17回日本蛋白質科学会年会, Jun. 2017. 松下夏樹, 松下佐知, 坂根亜由子, 佐々木卓也, 今村健志 :
非組込型レンチウイルスベクターを用いたCRISPR/Cas9システムによる高効率遺伝子ターゲティング,
第37回日本分子生物学会年会, 2014年11月. 坂根亜由子, 西村将臣, 吉澤信, 横田秀夫, 佐々木卓也 :
集団的細胞運動において1分子の構造変化がつくりだす秩序と法則,
第87回日本生化学会大会, 2014年10月. 坂根亜由子, 西村将臣, 横田秀夫, 佐々木卓也 :
集団的細胞運動においてJRABがつくりだす秩序と法則性,
第73回日本癌学会総会, 2014年9月. 坂根亜由子, 西村将臣, 吉澤信, 横田秀夫, 佐々木卓也 :
集団的細胞運動においてRab13-JRAB系がつくりだす秩序と法則性,
第66回日本細胞生物学会, 2014年6月. 坂根亜由子, 佐々木卓也 :
動く細胞,
ViEW2012ビジョン技術の実利用ワークショップ, 2012年12月. 坂根亜由子, 佐々木卓也 :
細胞接着・運動においてRab13-JRAB系が制御する小胞輸送とアクチン細胞骨格再編成,
第70回日本癌学会学術総会, 2011年10月. 坂根亜由子, 佐々木卓也 :
細胞間接着形成過程においてJRABが制御する細胞内小胞輸送とアクチン細胞骨格系の細胞膜直下でのクロストーク機構,
第63回日本細胞生物学会大会, 2011年6月. Takuya Sasaki and Ayuko Sakane :
Functions of Rab family small G proteins in neurite outgrowth.,
第62回日本細胞生物学会大会シンポジウム, May 2010. Tabata Keisuke, Matsunaga Kohichi, Ayuko Sakane, Takuya Sasaki, Noda Takeshi and Yoshimori Tamotsu :
The Rubicon family negatively regulates the endocytic pathway through the interactions with Rab7.,
The 62rd Annual Meeting of the Japan Society for Cell Biology, May 2010. Noriyuki Nishimura and Takuya Sasaki :
Rab8/13-JRAB/MICAL-L2 complexes control epithelial apical junctions.,
BMB2008(第31回日本分子生物学会年会・第81回日本生化学会大会合同大会, Dec. 2008. Takuya Sasaki and Ayuko Sakane :
Exocytotic Rab small G proteins regulate neuronal development and plasticity.,
BMB2008(第31回日本分子生物学会年会・第81回日本生化学会大会合同大会, Dec. 2008. 佐々木卓也, 西村範行, 坂根亜由子 :
高次細胞機能発現におけるエキソサイトーシス系Rabファミリー低分子量G蛋白質の作用機構,
第60回日本細胞生物学会大会, 2008年6月. 西村範行, 中逵弘能, 山村里恵, 佐々木卓也 :
Rab13結合蛋白質JRAB/MICAL-12とactinin-4による上皮細胞極性化の制御機構,
第30回日本分子生物学会年会・第80回日本生化学会大会合同大会, 2007年12月. 東尾浩典, 西村範行, 石崎宏好, 三好淳, 織田聡, 坂根亜由子, 佐々木卓也 :
マスト細胞の調節性分泌におけるDoc2α-Munc13-4系の役割,
第30回日本分子生物学会年会・第80回日本生化学会大会合同大会, 2007年12月. 中逵弘能, 西村範行, 山村里恵, 金山博臣, 佐々木卓也 :
Actinin-4によるJRAB/MICAL-L2の細胞膜局在の制御機構,
第66回癌学会学術総会, 2007年10月. 山村里恵, 西村範行, 中逵弘能, 荒瀬誠治, 佐々木卓也 :
タイトジャンクションとアドへレンスジャンクションの形成におけるJRAB/MICAL-L2,
第66回癌学会学術総会, 2007年10月. 坂根亜由子, 三好淳, 田中滋康, 松崎利也, 苛原稔, 石崎宏好, 岡本三紀, 高井義美, 佐々木卓也 :
Rab3低分子量G蛋白質ファミリーによる視床下部-下垂体-性腺系の制御,
第80回日本内分泌学会学術総会, 2007年6月. 中逵弘能, 西村範行, 山村里恵, 金山博臣, 佐々木卓也 :
JRAB/MICAL-L2の細胞膜局在におけるactinin-4の役割,
第59回日本細胞生物学会, 2007年5月. 山村里恵, 西村範行, 中逵弘能, 荒瀬誠治, 佐々木卓也 :
JRAB/MICAL-L2とRab8/13によるタイトジャンクションとアドヘレンスジャンクションの制御機構,
第59回日本細胞生物学会, 2007年5月. 東尾浩典, 西村範行, 石崎宏好, 三好淳, 坂根亜由子, 佐々木卓也 :
マスト細胞の調節性分泌におけるDoc2の役割,
第59回日本細胞生物学会, 2007年5月. 神田郁乃, 中西秀樹, 西村範行, 佐々木卓也 :
上皮細胞の接着・遊走におけるRab13の機能解析,
第15回日本形成外科学会基礎学術集会, 2006年10月. 神田郁乃, 西村範行, 寺井智也, 中西秀樹, 佐々木卓也 :
上皮細胞の細胞分散(cell scattering)におけるRab13-JRAB系の役割,
第65回日本癌学会総会, 2006年9月. 西村範行, 寺井智也, 神田郁乃, 佐々木卓也 :
Rab13結合蛋白質JRABによるタイトジャンクション形成の制御機構,
第65回日本癌学会総会, 2006年9月. 坂根亜由子, 真鍋進治, 石崎宏好, 岡本三紀, 吉田隆行, 三好淳, 神谷温之, 高井義美, 佐々木卓也 :
Rab3GAPによるシナプス伝達と可塑性の制御,
第28回日本分子生物学会年会, 2005年12月. 西村範行, 寺井智也, 神田郁乃, 佐々木卓也 :
タイトジャンクションにおけるRab13低分子量G蛋白質の標的蛋白質JRABの単離と機能解析,
第28回日本分子生物学会年会, 2005年12月. 五石圭一, 水野広一, 中西秀樹, 佐々木卓也 :
抗原刺激によるrat basophilic leukemia-2H3細胞からのヒスタミン遊離におけるRab27低分子量G蛋白質の役割,
第27回日本分子生物学会年会, 2004年12月. 西村範行, 寺井智也, 坂根亜由子, 神田郁乃, 佐々木卓也 :
Rabファミリー低分子量G蛋白質による細胞極性・接着の制御機構,
第45回日本生化学会中国・四国支部例会, 2004年5月. 森本慎也, 西村範行, 佐々木卓也, 田代征記 :
Rabファミリー低分子量G蛋白質Rab13によるタイトジャンクションの接着分子Occludinの小胞輸送制御機構,
第104回日本外科学会学術集会, 2004年4月. 水野広一, 北村明子, 佐々木卓也 :
Rab8低分子量G蛋白質の新規標的蛋白質Rabring8の同定と機能解析,
第26回日本分子生物学会年会, 2003年12月. 真鍋進治, 西村範行, 佐々木卓也, 永廣信治 :
血液脳関門を支える細胞間接着分子の小胞輸送の制御機構,
第4回日本分子脳神経外科学会, 2003年9月. 森本慎也, 西村範行, 北村明子, 品原和加子, 山本恭代, 寺井智也, 坂根亜由子, 真鍋進治, 田代征記, 佐々木卓也 :
Rabファミリー低分子量G蛋白質によるタイトジャンクション膜蛋白質の小胞輸送の制御機構,
第62回日本癌学会総会, 2003年9月. 佐々木卓也, 西村範行 :
細胞極性と接着を支える小胞輸送の制御機構:Rabファミリー低分子量G蛋白質の役割,
第56回日本細胞生物学会大会ワークショップ, 2003年5月. 佐々木卓也, 西村範行, 水野広一, 三好淳, 高井義美 :
Rabファミリー低分子G蛋白質によるexocytosisの制御機構,
第25回日本分子生物学会年会ワークショップ, 2002年12月. 北村明子, 水野広一, 佐々木卓也 :
Rab7低分子量G蛋白質の新規標的蛋白質Rabring7の同定と機能解析,
第25回日本分子生物学会年会, 2002年12月. 佐々木卓也, 西村範行, 水野広一, 三好淳, 中西宏之, 高井義美 :
Rab低分子G蛋白質によるエキソサイトーシスの制御機構,
第75回日本生化学会大会シンポジウム, 2002年10月. 水野広一, 北村明子, 佐々木卓也 :
CytoTrap^TM法を用いた新規Rab7標的蛋白質Rabring7の同定と機能解析,
第75回日本生化学会大会シンポジウム, 2002年10月. 山本恭代, 西村範行, 森本慎也, 北村明子, 真鍋進治, 佐々木卓也 :
Rab3BとRab13低分子G蛋白質によるゴルジ体—細胞膜間小胞輸送の制御機構,
第75回日本生化学会大会, 2002年10月. 佐々木卓也, 三好淳, 中西宏之, 高井義美 :
Rab低分子G蛋白質とその関連蛋白質による小胞輸送の制御機構,
第74回日本生化学会大会シンポジウム, 2001年10月. 高井義美, 中西宏之, 佐々木卓也, 三好淳 :
Rab3A低分子G蛋白質による神経伝達物質放出の調節機構,
第78回日本生理学会大会シンポジウム, 2001年3月. 佐々木卓也, 三好淳, 中西宏之, 高井義美 :
Rab低分子量G蛋白質とその関連蛋白質による小胞輸送の制御機構,
第23回日本分子生物学会年会シンポジウム, 2000年12月. 佐々木卓也, 三好淳, 中西宏之, 高井義美 :
Rab3A低分子量G蛋白質とその活性制御蛋白質による神経伝達物質放出の調整機構,
第53回日本細胞生物学会大会シンポジウム, 2000年10月. 佐々木卓也, 三好淳, 中西宏之, 高井義美 :
Rab3A低分子量G蛋白質の活性制御蛋白質による神経伝達物質放出の調節機構,
第73回日本生化学会大会シンポジウム, 2000年10月. 金永満, 萬本明子, 佐々木卓也, 高井義美 :
Rab11低分子量G蛋白質の標的蛋白質Rab11BP/Rabphilin11による小胞のリサイクリングの制御機構,
第73回日本生化学会大会, 2000年10月. 石崎宏好, 三好淳, 戸川温, 田中三紀, 神谷温之, 小澤瀞司, 阪口岳, 佐々木卓也, 高井義美 :
Rab GDIa欠損マウスの表現型解析:Rab GDIaの神経伝達物質放出に対する抑制作用,
第22回日本分子生物学会年会, 1999年12月. 萬本明子, 發田郁子, 大塚稔久, 佐々木卓也, 高井義美 :
低分子量G蛋白質Rab11の標的蛋白質rabphilin-11の精製と性状解析,
第72回日本生化学会大会, 1999年10月. 佐々木卓也, 織田聡, 三好淳, 高井義美 :
Rab3系とDoc2系による神経伝達物質放出の調整機構,
第52回日本細胞生物学会大会シンポジウム, 1999年8月. 匂坂敏朗, 的崎尚, 高石健司, 佐々木卓也, 高井義美 :
細胞の接着と運動におけるRhoとRab低分子量G蛋白質ファミリーの協調作用,
第52回日本細胞生物学会大会シンポジウム, 1999年8月. 阪口岳, 織田聡, 内藤陽, 前田美幾, 五十嵐久永, 佐々木卓也, 高井義美 :
Munc13と結合する新規の脳特異的スペクトリンの同定とその性状解析,
第71回日本生化学会大会, 1998年10月. 永野史子, 織田聡, 阪口岳, 前田美幾, 渡部剛, 内山安男, 佐々木卓也, 高井義美 :
Doc2と細胞質ダイニンの連鎖Tctex-1の相互作用とその機能解析,
第71回日本生化学会大会, 1998年10月. 高井義美, 佐々木卓也, 織田聡, 阪口岳, 高橋智幸, 真鍋俊也, 小林克典, 持田澄子 :
神経伝達物質の放出と長期増強の形成におけるDoc2の役割と作用機構,
第21回日本神経科学・第41回日本神経化学合同大会, 1998年9月. 高井義美, 佐々木卓也, 高石健司 :
細胞の接着と運動の制御機構,
第57回日本癌学会総会シンポジウム, 1998年9月. 中野克俊, 高石健司, 今村博司, 児玉昌子, 佐々木卓也, 高井義美 :
細胞運動におけるアクチン細胞骨格の再編成 — RhoとRab低分子量G蛋白質ファミリーによる制御機構,
第57回日本癌学会総会, 1998年9月. 前田賢人, 月田早智子, 佐々木卓也, 高井義美, 今村正之, 月田承一郎 :
メルリンとRho GDIとの相互作用,
第57回日本癌学会総会, 1998年9月. 田中一馬, 佐々木卓也, 高井義美 :
Rho低分子量G蛋白質ファミリーによるアクチン細胞骨格系の時間的・空間的制御,
第20回日本分子生物学会年会シンポジウム, 1997年12月. 佐々木卓也, 白瀧博通, 織田聡, 高井義美 :
Rab3-Rabphilin3系とDoc2-Munc13系による神経伝達物質の放出機構,
第20回日本分子生物学会年会シンポジウム, 1997年12月. 高石健司, 佐々木卓也, 高井義美 :
Rho低分子量ファミリーによる細胞接着の制御,
第20回日本分子生物学会年会シンポジウム, 1997年12月. 朝倉剛, 佐々木卓也, 永野史子, 佐藤綾子, 尾葉石浩, 西岡秀夫, 今村博司, 田中一馬, 中西宏之, 高井義美 :
出芽酵母の新規アクチン結合蛋白質の単離と性状解析,
第20回日本分子生物学会年会, 1997年12月. 内藤陽, 織田聡, 坂口岳, 前田美幾, 五十嵐久永, 佐々木卓也, 高井義美 :
神経伝達物質放出過程におけるDoc2とMunc13の作用機構,
第20回日本分子生物学会年会, 1997年12月. 永野史子, 佐々木卓也, 金子善興, 福井浩司, 今住克則, 高井義美 :
Rab3低分子量G蛋白質サブファミリー特異的GTPase活性促進蛋白質(Rab3 GAP)のクローニングと性状解析,
第70回日本生化学会大会, 1997年9月. 大屋健, 佐々木卓也, 加藤正樹, 高井義美 :
Rab5-Rabaptin5系を介したRabphilin3によるエンドサイトーシスの制御,
第70回日本生化学会大会, 1997年9月. 高石健司, 佐々木卓也, 西岡秀夫, 高井義美 :
RhoとRho低分子量G蛋白質による細胞接着の制御,
第56回日本癌学会総会, 1997年9月. 高橋和男, 佐々木卓也, 萬本明子, 高石健司, 月田承一郎, 月田早智子, 高井義美 :
ERMファミリーによるRho低分子量G蛋白質の活性化機構,
第56回日本癌学会総会, 1997年9月. 海川正人, 田中一馬, 清水一也, 今村博司, 亀井尚, 佐々木卓也, 高井義美 :
Rho低分子量G蛋白質の標的蛋白質BNI1に結合するF-アクチン結合蛋白質,
第56回日本癌学会総会, 1997年9月. 佐々木卓也, 白瀧博通, 織田聡, 高井義美 :
C1およびC2ドメインとCa²⁺依存性エクソサイトーシス,
第70回日本内分泌学会年次学術総会シンポジウム, 1997年6月. 高井義美, 田中一馬, 佐々木卓也, 白瀧博通 :
低分子量G蛋白質を介するシグナル伝達機構,
第55回日本癌学会総会シンポジウム, 1996年10月. 高橋和男, 佐々木卓也, 萬本明子, 高石健司, 月田承一郎, 月田早智子, 高井義美 :
低分子量G蛋白質RhoとERMファミリー,
第55回日本癌学会総会, 1996年10月. 松田修二, 佐々木卓也, 田中一馬, 中西宏之, 尾崎公美, 高井義美 :
低分子量G蛋白質Rhoの活性制御蛋白質,
第55回日本癌学会総会, 1996年10月. 田中一馬, 佐々木卓也, 高井義美 :
低分子量G蛋白質Rhoの活性制御蛋機構と作用機構,
第69回日本生化学会・第19回日本分子生物学会合同年会シンポジウム, 1996年8月. 佐々木卓也, 白瀧博通, 中西宏之, 高井義美 :
Rab3と神経伝達物質の放出機構,
第69回日本生化学会・第19回日本分子生物学会合同年会シンポジウム, 1996年8月. 坂口岳, 織田聡, 内藤陽, 前田美幾, 五十嵐久永, 佐々木卓也, 高井義美 :
Doc2アイソフォームの単離とその性状解析,
第69回日本生化学会・第19回日本分子生物学会合同年会, 1996年8月. 高井義美, 田中一馬, 佐々木卓也 :
RasおよびRho低分子量G蛋白質の標的蛋白質,
第18回日本分子生物学会年会シンポジウム, 1995年12月. 福井浩司, 藤田恭之, 木村敏啓, 佐々木卓也, Sdhof C. Thomas, Scheller Richard, 高井義美 :
Protein Kinase C (PKC)によるMunc-18/n-Sec1/rbSec1のリン酸化とその意義,
第18回日本分子生物学会年会, 1995年12月. 小室竜太郎, 佐々木卓也, 織田聡, 高井義美 :
PC12細胞のCa²⁺ 依存性分泌におけるRabphilin-3Aの生理機能の解析,
第18回日本分子生物学会年会, 1995年12月. 織田聡, 佐々木卓也, 内藤陽, 小室竜太郎, 阪口岳, 前田美幾, 五十嵐久永, 高井義美 :
2つのC2領域を有する新しい蛋白質Doc2の単離とその生理機能の解析,
第18回日本分子生物学会年会, 1995年12月. 高石健司, 佐々木卓也, 高橋和男, 月田承一郎, 月田早智子, 高井義美 :
Rhoによる細胞間接着及び細胞質分裂の制御機構,
第54回日本癌学会総会, 1995年10月. 高井義美, 佐々木卓也, 白瀧博通, 中西宏之 :
Rab3A低分子量Gタンパク質と神経伝達物質の放出機構,
第48回日本細胞生物学会シンポジウム, 1995年10月. 佐々木卓也, 白瀧博通, 中西宏之, 高井義美 :
低分子量G蛋白質と細胞内小胞輸送,
第68回日本生化学会大会シンポジウム, 1995年9月. 今住克則, 佐々木卓也, 荒木敬司, 平野尚伸, 中西宏之, 高井義美 :
Rab3A GTPase活性促進蛋白質(Rab3A GAP)の精製と性状解析,
第68回日本生化学会大会, 1995年9月. 荒木敬司, 白瀧博通, 平野尚伸, 加藤正樹, 佐々木卓也, 高井義美 :
新しいRab GDP解離抑制蛋白質(Rab GDIb)の精製と性状解析,
第68回日本生化学会大会, 1995年9月. 栗原秀夫, 横関健昭, 多胡憲治, 森井成人, 成宮周, 佐々木卓也, 高井義美, 堅田利明, 金保安則 :
低分子量GTP結合蛋白質RhoによるPhospholipase Dの活性化,
第68回日本生化学会大会, 1995年9月. 白瀧博通, 佐々木卓也, 高井義美 :
低分子量GTP結合蛋白質と小胞輸送,
第24回日本医学会総会シンポジウム, 1995年4月. 高井義美, 佐々木卓也, 田中一馬, 白瀧博通, 中西宏之, 黒田真也 :
Rasスーパーファミリーとがん細胞の増殖・転移機構,
第53回日本癌学会総会シンポジウム, 1994年10月. 高石健司, 佐々木卓也, 西山隆之, 亀山毅明, 高井義美 :
HGFとTPAによるRhoの活性化と細胞膜のRuffling領域へのTranslocation,
第53回日本癌学会総会, 1994年10月. 田中一馬, 佐々木卓也, 中西宏之, 高井義美 :
低分子量G蛋白質と細胞内シグナリング,
第67回日本生化学会大会シンポジウム, 1994年9月. 佐々木卓也, 白瀧博通, 田中一馬, 中西宏之, 高井義美 :
小胞輸送と低分子量GTP結合タンパク質,
第47回日本細胞生物学会大会シンポジウム, 1994年9月. 高橋和男, 佐々木卓也, 荒木敬司, 宮崎章, 高井義美 :
MSS4とRab3A GRF GDP/GTP交換反応促進蛋白質の性状比較,
第67回日本生化学会大会, 1994年9月. 藤田恭之, 佐々木卓也, 高橋和男, 今住克則, 荒木敬司, 加藤正樹, 高井義美 :
Rabphilin-3AのGDP/GTP交換反応促進活性,
第67回日本生化学会大会, 1994年9月. 今住克則, 佐々木卓也, 高橋和男, 荒木敬司, 加藤正樹, 高井義美 :
Rabphilin-3A結合蛋白質の同定,
第67回日本生化学会大会, 1994年9月. 高井義美, 佐々木卓也, 田中一馬, 中西宏之, 黒田真也 :
細胞増殖と細胞内シグナル伝達,
第31回日本臨床代謝学会総会シンポジウム, 1994年4月. 白瀧博通, 貝淵弘三, 佐々木卓也, 田中一馬, 中西宏之, 高井義美 :
神経伝達物質の放出におけるRab3Aの作用機構,
第67回日本薬理学会年会シンポジウム, 1994年3月. 高井義美, 貝淵弘三, 佐々木卓也, 田中一馬, 白瀧博通, 中西宏之 :
RasとRhoの機能と作用機構,
第16回日本分子生物学会年会シンポジウム, 1993年12月. 白瀧博通, 貝淵弘三, 佐々木卓也, 田中一馬, 中西宏之, 高井義美 :
Rab3A-Rabphilin-3A系と神経伝達物質の放出機構,
第16回日本分子生物学会年会シンポジウム, 1993年12月. 佐々木卓也, 貝淵弘三, 田中一馬, 白瀧博通, 高井義美 :
rasスーパーファミリーの機能と作用機構,
第52回日本癌学会総会シンポジウム, 1993年10月. 白瀧博通, 貝淵弘三, 佐々木卓也, 高井義美 :
Rabと細胞内小胞輸送,
第46回日本細胞生物学会大会シンポジウム, 1993年10月. 高石健司, 佐々木卓也, 加藤正樹, 矢持亘, 西山隆之, 黒田真也, 高井義美 :
rho p21とHGFによる細胞運動の制御,
第52回日本癌学会総会, 1993年10月. 西山隆之, 佐々木卓也, 高石健司, 黒田真也, 加藤正樹, 高井義美 :
rho p21と細胞増殖因子による細胞膜のrufflingの制御,
第52回日本癌学会総会, 1993年10月. 加藤正樹, 佐々木卓也, 高井義美 :
Rho GDIによるRhoとRacの活性制御機構,
第66回日本生化学会大会, 1993年10月. 清水一也, 貝淵弘三, 黒田真也, 織田聡, 佐々木卓也, 高井義美 :
Smg GDSとDblによるRhoの活性化機構,
第66回日本生化学会大会, 1993年10月. 貝淵弘三, 佐々木卓也, 田中一馬, 白瀧博通, 高井義美 :
低分子量G蛋白質と細胞機能,
第70回日本生理学会大会シンポジウム, 1993年4月. 白瀧博通, 貝淵弘三, 菊池章, 佐々木卓也, 高井義美 :
低分子量G蛋白質と神経伝達物質遊離機構,
第16回日本神経科学学会シンポジウム, 1992年12月. 貝淵弘三, 菊池章, 佐々木卓也, 田中一馬, 高井義美 :
ras p21を介する細胞内情報伝達機構,
第15回日本分子生物学会年会シンポジウム, 1992年12月. 岸清彦, 佐々木卓也, 伊藤孝仁, 黒田真也, 貝淵弘三, 高井義美 :
細胞質分裂における低分子量G蛋白質rho p21によるアクトミオシン系の制御,
第15回日本分子生物学会年会, 1992年12月. 前田彰男, 貝淵弘三, 佐々木卓也, 高井義美 :
低分子量G蛋白質rho p21のGDP解離抑制蛋白質のヒトcDNAのクロ-ニング,
第15回日本分子生物学会年会, 1992年12月. 浅田全範, 貝淵弘三, 佐々木卓也, 高井義美 :
低分子量G蛋白質smg p25/rab3 p25のGDP解離抑制蛋白質(smg p25 GDI)のヒトcDNAのクロ-ニング,
第15回日本分子生物学会年会, 1992年12月. 高井義美, 貝淵弘三, 菊池章, 佐々木卓也 :
ras p21とその類似低分子量G蛋白質,
第65回日本生化学会大会シンポジウム, 1992年10月. 高井義美, 貝淵弘三, 菊池章, 佐々木卓也 :
低分子量Gタンパク質と細胞骨格制御,
第45回日本細胞生物学会大会シンポジウム, 1992年10月. 夜久英明, 佐々木卓也, 平田健一, 増田忠之, 黒田真也, 岸清彦, 菊池章, 貝淵弘三, 松浦善治, 関ひとみ, 斎田孝市, 高井義美 :
血管平滑筋の収縮における低分子量G蛋白質, rho p21, の作用機構,
第65回日本生化学会大会, 1992年10月. 黒田真也, 菊池章, 佐々木卓也, 小谷圭, 松浦善治, 高井義美 :
rho GDIとsmg GDSによるrho p21低分子量GTP結合蛋白質活性の二重制御,
第51回日本癌学会総会, 1992年9月. 伊藤孝仁, 貝渕弘三, 白瀧博通, 畑裕, 河村史朗, 廣吉基己, 佐々木卓也, 高井義美 :
低分子量GTP結合蛋白質smg p21の活性調節機構,
第64回日本生化学会大会, 1991年10月. 小谷圭, 貝渕弘三, 白瀧博通, 廣吉基己, 磯村光男, 荒木伸, 佐々木卓也, 菊池章, 高井義美 :
低分子量GTP結合蛋白質smg p21Bの翻訳後修飾のsmg GDS作用における役割,
第64回日本生化学会大会, 1991年10月. 佐々木卓也, 貝淵弘三, Kabcenell A.K., Novick P.J., 高井義美 :
smg p25A GDIのSEC4蛋白質に対する影響,
第64回日本生化学会大会, 1991年10月. 廣吉基己, 貝渕弘三, 白瀧博通, 佐々木卓也, 磯村光男, 山本武司, 菊池章, 高井義美 :
ras p21類似GTP結合蛋白質，smg p21BのC末端ペプチドのsmg GDS阻害作用,
第50回日本癌学会総会, 1991年9月. 水野敬和, 貝淵弘三, 河村元博, 山本武司, 佐古田剛, 藤岡宏幸, 佐々木卓也, 伊藤孝仁, 松浦善治, 高井義美 :
Ki-ras p21のリン酸化と活性調節機構,
第50回日本癌学会総会, 1991年9月. 佐々木卓也, 貝淵弘三, 荒木伸, 高井義美 :
smg p25Aの機能ドメイン,
第63回日本生化学会大会, 1990年9月. 畑裕, 菊池章, 佐々木卓也, 高井義美 :
ras p21 GAPによるras p21 のGTPase 活性促進作用に対するsmg p21の抑制効果,
第49回日本癌学会総会, 1990年7月. 佐々木卓也, 菊池章, 荒木伸, 畑裕, 磯村光男, 高井義美 :
低分子量GTP結合蛋白質smg p25AのGDP解離促進蛋白質,
第62回日本生化学会大会, 1989年11月. 畑裕, 佐々木卓也, 菊池章, 高井義美 :
ras p21 類似低分子量GTP結合蛋白質に対するGTPase activating protein(GAP)の基質特異性,
第62回日本生化学会大会, 1989年11月. 荒木伸, 菊池章, 佐々木卓也, 畑裕, 高井義美 :
smg p21 特異的GTPase-activating protein(GAP)の精製と性状,
第48回日本癌学会総会, 1989年10月.

研究会・報告書: 研究者総覧に該当データはありませんでした。

特許: 研究者総覧に該当データはありませんでした。
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補助金・競争的資金: アクチン細胞骨格制御における蛋白質の構造ダイナミクスとdisorder領域の役割 (研究課題/領域番号: 21K06838 )
１分子構造変化をターゲットとしたがん浸潤・転移の克服に向けた診断・治療戦略 (研究課題/領域番号: 15K15084 )
神経回路形成に関与するRabファミリー低分子量G蛋白質の機能と作用機構 (研究課題/領域番号: 21390082 )
「細胞内ロジスティクス：病態の理解に向けた細胞内物流システムの融合研究」の運営 (研究課題/領域番号: 20113001 )
がんの浸潤・転移に関わる細胞間接着分子の小胞輸送の制御機構 (研究課題/領域番号: 20013031 )
高次神経機能を支えるロジスティクス機構の解明 (研究課題/領域番号: 20113004 )
シグナル伝達の時・空間的制御を支えるRabファミリー低分子量G蛋白質の作用機構 (研究課題/領域番号: 18390089 )
Rabファミリー低分子量G蛋白質による高次機能システムを支える小胞輸送の制御機構 (研究課題/領域番号: 15390096 )
多細胞生物の可塑性を支える小胞輸送の制御機構 (研究課題/領域番号: 15079207 )
がん細胞の浸潤・転移における小胞輸送の役割の解明 (研究課題/領域番号: 14028045 )
細胞運動に関わるインテグリンの小胞輸送の制御機構 (研究課題/領域番号: 13877017 )
シナプス可塑性に関与するRabファミリー低分子量G蛋白質の機能と作用機構 (研究課題/領域番号: 13470025 )
膜結合型増殖因子と受容体型チロシンキナーゼを介したがん細胞の浸潤制御機構 (研究課題/領域番号: 13216057 )
細胞増殖のシグナリング機構 (研究課題/領域番号: 12215079 )
低分子量G蛋白質によるの細胞の接着と運動の制御機構 (研究課題/領域番号: 11680632 )
神経シナプス小胞輸送の分子機構―記憶形成の理解に向けて (研究課題/領域番号: 10215204 )
記憶形成におけるRab3A系とDoc2系の機能と作用機構 (研究課題/領域番号: 10155214 )
低分子量G蛋白質の活性制御機構と作用機構 (研究課題/領域番号: 10044285 )
Ca^<2+>・リン脂質結合領域(C2様領域)を有する新しい蛋白質の機能と作用機構 (研究課題/領域番号: 09670153 )
神経伝達物質の放出反応におけるRab3A系の役割と作用機構 (研究課題/領域番号: 09670126 )
Rho低分子量G蛋白質とその関連蛋白質の機能修飾物質のスクリーニング系の開発 (研究課題/領域番号: 09557011 )
シナプスにおける新しいCa^<2+>センサーの機能と作用機構 (研究課題/領域番号: 09259220 )
神経伝達物質の放出におけるRab3A-Rabphilin-3A系の機能と作用機構 (研究課題/領域番号: 08680706 )
Ca^<2+>・リン脂質結合領域(C_2)を有する新しい蛋白質の機能と作用機構 (研究課題/領域番号: 08670147 )
シナプスにおける新しいCa^<2+>センサーの機能と作用機構 (研究課題/領域番号: 08270241 )
低分子量G蛋白質Rhoの活性化機構と作用機構 (研究課題/領域番号: 07770103 )
神経伝達物質の放出機構におけるRab3A低分子量G蛋白質系の機能と作用機構 (研究課題/領域番号: 07279225 )
シナプスにおける新しいCa^<2+>センサーの機能と作用機構 (研究課題/領域番号: 07278245 )
C_2様領域を持つ新しい蛋白質Rabphilin-3AとDoc2の機能と作用機構 (研究課題/領域番号: 07268212 )
低分子量G蛋白質Rhoの活性化機構と作用機構 (研究課題/領域番号: 06770083 )
低分子量G蛋白質とその関連蛋白質の機能修飾物質の開発およびその有効利用 (研究課題/領域番号: 06557012 )
低分子量G蛋白質による細胞機能の制御機構 (研究課題/領域番号: 06404021 )
細胞の増殖・分化のシグナルの伝達機構 (研究課題/領域番号: 06283221 )
細胞質分裂における低分子量G蛋白質Rhoの機能と作用機構 (研究課題/領域番号: 06275207 )
プレ・ポストシナプスの相互作用における低分子量G蛋白質の役割と作用機構 (研究課題/領域番号: 06253220 )
アメリカ大陸を中心としたがん研究先進グループとの研究交流 (研究課題/領域番号: 06042003 )
rho p21 GTP結合蛋白質による細胞骨格の制御機構とその病態 (研究課題/領域番号: 05770097 )
血管平滑筋細胞における血管作動物質のシグナル伝達と低分子量GTP結合蛋白質 (研究課題/領域番号: 05670616 )
蛋白質の選別輸送における低分子量GTP結合蛋白質の機能と作用機構 (研究課題/領域番号: 05252222 )
細胞内情報伝達系と細胞増殖の制御機構 (研究課題/領域番号: 04253229 )
神経伝達物質放出における低分子量GTP結合蛋白質の機能と作用機構 (研究課題/領域番号: 04267215 )
蛋白質の選別輸送における低分子量GTP結合蛋白質の機能と作用機構 (研究課題/領域番号: 04259218 )
低分子量GTP結合蛋白質の機能修飾物質の開発と有効利用 (研究課題/領域番号: 03558019 )
低分子量GTP結合蛋白質を介する細胞内情報伝達機構とその病態 (研究課題/領域番号: 03404022 )
アメリカ大陸を中心としたがん研究先進グループとの研究交流 (研究課題/領域番号: 03042013 )
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専門分野・研究分野: 生化学 (Biochemistry)
分子生物学 (Molecular Biology)
細胞生物学 (Cell Biology)
所属学会・所属協会: 日本癌学会
日本分子生物学会
日本細胞生物学会
日本生化学会
秀潤社「細胞工学」Vol.28 No.12
委員歴・役員歴: 日本生化学会 (評議員)
秀潤社「細胞工学」Vol.28 No.12 (監修 [2009年12月])
受賞: 1998年10月, 日本癌学会奨励賞 (日本癌学会)
活動: 動物実験委員会委員 (2006年4月〜2014年3月)
自己点検·評価委員会委員 (2012年4月〜2014年3月)
学部長補佐 (2013年4月〜2014年3月)
入学試験委員会委員 (2013年5月〜2014年4月)

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Jグローバル最終確認日: 2024/4/20 01:22
氏名（漢字）: 佐々木卓也
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氏名（英字）: Sasaki Takuya
所属機関: 徳島大学教授

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researchmap最終確認日: 2024/4/21 01:36
氏名（漢字）: 佐々木卓也
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ＫＡＫＥＮで最新データを確認する

2024年4月20日更新

研究者番号: 40241278

所属（現在）: 2024/4/1 : 徳島大学, 大学院医歯薬学研究部(医学域), 教授

所属（過去の研究課題 情報に基づく）*注記: 2021/4/1 – 2022/4/1 : 徳島大学, 大学院医歯薬学研究部(医学域), 教授
2016/4/1 : 徳島大学, 大学院医歯薬学研究部(医学系), 教授
2015/4/1 : 徳島大学, 大学院医歯薬学研究部, 教授
2012/4/1 : 徳島大学, ヘルスバイオサイエンス研究部, 教授
2006/4/1 – 2012/4/1 : 徳島大学, 大学院・ヘルスバイオサイエンス研究部, 教授
2005/4/1 – 2006/4/1 : 徳島大学, 大学院ヘルスバイオサイエンス研究部, 教授
2004/4/1 : 徳島大学, 医学部, 教授
2004/4/1 : 徳島大学, 大学院・ヘルスバイオサイエンス研究部, 教授
2001/4/1 – 2003/4/1 : 徳島大学, 医学研究科, 教授
2000/4/1 – 2001/4/1 : 徳島大学, 医学部, 教授
1999/4/1 : 大阪大学, 医学系研究科, 助教授
1998/4/1 : 大阪大学, 医学部, 助教授
1994/4/1 – 1998/4/1 : 大阪大学, 医学部, 助手
1992/4/1 – 1993/4/1 : 神戸大学, 医学部, 助手

審査区分/研究分野

研究代表者

医学 / 生理 / 病態医化学
医学 / 生理 / 医化学一般
生物系 / 医歯薬学 / 基礎医学 / 医化学一般
複合領域 / 生物化学 / 機能生物化学
生物系 / 医歯薬学 / 基礎医学 / 病態医化学
生物系

研究代表者以外

医学 / 内科 / 循環器内科学
複合領域 / 生物化学 / 機能生物化学
医学 / 生理 / 病態医化学
複合領域 / 生物化学 / 代謝生物化学
医学 / 生理 / 医化学一般
生物系
小区分48040:医化学関連

キーワード

研究代表者

低分子量GTP結合蛋白質 / smp p25A / rab3A p25 / 細胞内小胞輸送 / regulated secretion / rabphilin / アクティブゾーン / シナプトタグミン / 低分子量G蛋白質 / Rab3A / RabGDI / トランスロケーション / Rabphilin-3A / シナプス / 神経伝達物質 / Rho / Rho GDI / Smg GDS / Rac / Dbl / Cdc42 / 翻訳後修飾 / 細胞質分裂 / 収縮環 / ERMファミリー / CD44 / アクチンフィラメント / 細胞膜ラッフリング / Db1 / C2様領域 / Doc2 / Ca^<2+> / シナプス小胞 / アンカリング蛋白質 / 機能領域 / Ca^<2+>センサー / アクチン細胞骨格 / adherens junction / tight junction / E-カドヘリン / ZO-1 / α-アクチニン / C2領域 / 浸潤・転移 / 細胞間接着分子 / 小胞輸送 / クローディン / タイトジャンクション / Rabファミリー / インテグリン / Rab / 活性制御蛋白質 / scaffold蛋白質 / 可塑性 / 神経伝達 / 細胞接着 / Rabファミリー低分子量GTPase / Rabconnection-3 / Rab13 / JRAB / 低分子量CTPase / Rab3 GAP / Rabファミリー低分子量G蛋白質 / 接着分子 / claudin / occludin / 高次神経機能 / 組織・器官形成 / 細胞間接着 / Rab8 / アドヘレンスジャンクション / Actinin-4 / シナプス形成 / 神経突起形成 / ノックアウトマウス / 細胞内物流システム / Rabconnectin-3 / PC12細胞 / 分子内結合 / 神経回路 / Rab3 / 神経回路形成 / KOマウス / 構造変化 / Rab3 GEP / long-term potentiation / Muncl3 / Rabaptin-5 / Munc13 / ダイニン / LTP / C2 domain / neurotransmitter release / シナプス小胞輸送 / Rab GDI / 神経伝達物質放出 / 呼吸不全 / 神経筋接合部 / Rab11 / Rabphilin-11 / mSec13 / Rab GDIα / X染色体性非特異的精神遅滞 / けいれん重積 / 微小管 / vesicle transport / neurotransmitter / 細胞運動 / リサイクリング / 細胞骨格 / Rhoファミリー低分子量G蛋白質 / cell migration / Rab family / microtubule / recycling / シナプス可塑性 / Rab3 GFP / グルタミン酸受容体 / synaptic plasticity / regulators / 高次機能 / Claudin / タイトジャクンション / vesicular transport / シグナル伝達 / 細胞増殖 / Rab7 / Rabファミリー低分子量G蛋自質 / Signal transduction / Rab proteins / neurotransmission / cell-cell adhesion / cell growth / Rab12 / がん浸潤・転移 / 集団的浸潤

研究代表者以外

低分子量G蛋白質 / Rho / HGF / 細胞運動 / Rho GDI / C3 / TPA感受性因子 / Cキナーゼ / 細胞増殖 / 低分子量GTP結合蛋白質 / ras p21 / rho p21 / smg GDS / rho GDI / smg p25a / ral3A p25 / rabphilin / シナプトタグミン / Ca^<2+>チャネル / アクティブゾーン / 血管平滑筋 / GTP結合蛋白質 / ras / MAPキナーゼ / rho / Rab3A / Rabphilin-3A / 神経伝達物質 / カルモデュリンキナーゼII / がん / Rab / アクチン細胞骨格 / 細胞内小胞輸送 / 浸潤・転移 / 細胞骨格 / ERM / BNI1 / CD44 / アクチン / Ras / B-Raf / 14-3-3蛋白質 / Smg GDS / ERM-CD44系 / Doc2 / Ca^<2+>センサー / Rab GDI / Rob3 GAP / Rab GDT / Rab3 GAP / Rabphilin3 / Tomosyn / Munc13 / SNARE / 記憶 / 放出反応 / dynein / 細胞接着 / ネクチン / Cdc42 / Rac / Necl-5 / Nectin-Afadin系 / Cadherin-Catenin系 / Nectin-Afadin / Frabin-Cdc42 / Gab-1 / Rab11 / Nectin-Afadin-Ponsin系 / Frabin-Cdc42系 / HB-EGF / Shedding / Transcriptional repressor / PLZF / Tight junction / cell adhesion molecule / claudin / shedding / repressor / EGF family / metalloprotease / ADAM / 胃がん / IL-8 / SH3蛋白質 / EGFファミリー / EGFRトランス活性化 / Tumor survival / Metalloprotease / Juxtacrine growth / メンブレントラフィック / 細胞内輸送 / 情報科学・工学 / ケミカルバイオロジー / 分子細胞生物学 / 情報発信 / 成果報告 / 社会還元 / オルガネラ / 画像解析 / 細胞内ロジスティクス / 病態の理解 / 融合研究 / アウトリーチ / 疾患 / 情報科学 / 高次生体システム / 研究情報交換 / がん遺伝子 / ウイルス発がん / 発がんプロモーター / がん抑制遺伝子 / がん細胞 / 増殖制御 / 転写調節 / がん研究 / 研究交流 / 北米 / 研究室訪問 / 研究集会 / Information exchange / Oncogene / Tumor virus / Tumor promoter / Tumor suppressor gene / Cancer cells / Growth control / Transcriptional regulation / CDC25Mm / REKS / smg p25A / rab3A p25 / 細胞内情報伝達機構 / 翻訳後修飾 / ゲラニルゲラニル基 / リン酸化 / 平滑筋 / 活性酸素 / small GTP-binding protein / rabphilin-3A / 活性制御蛋白質 / 標的蛋白質 / シナプス小胞 / プロテインキナーゼ / rac p21 / プレニル化 / C末端側ペプチド / ファルネシル基転移酵素 / ゲラニルゲラニル基転移酵素 / 国際学術 / 海外派遣 / 癌 / 細胞社会学 / シグナル伝達 / 細胞周期 / 薬品設計 / 遺伝子治療 / ウイルス発癌 / 癌治療 / 化学発癌 / 情報交換 / ドラッグデザイン / 癌遺伝子治療 / 癌化学療法 / International Scientific Research / Cancer / Information Exchange / Signal Transduction / Cell Cycle / Cell Adhesion / Drug Design / Gene Therapy / BNR1 / プロフィリン / PKC1 / Rabphi7in-3A / Small GTP-binding / The ERM family / Rap1 / SmgGDS / SMAP / 出芽酵母 / スクリーニング系 / 細胞壁 / スクリーニング法 / Budding yeast / Small GTP-binding protein / Actin cytoskeleton / Screening system / Cell wall / Rab3 GEP / Tomsyn / small G protein / neurotransmitter release / Rabphilin-11 / Frabin / BNT1 / RabGD1 / SHP-2 / SPA2 / mDia / ROCK / Small G Protein / アクチン細胞骨格制御 / 蛋白質の構造ダイナミクス / Disorder領域

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2021年11月18日

１分子の構造変化が制御するオルガネラダイナミクス　―オルガネラ膜変形の新たな分子機序の解明―

坂根亜由子佐々木卓也

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