トップ›研究者一覧›坂根亜由子

研究者を探す

研究者にアプローチする
更新情報を通知する

坂根亜由子

徳島大学

プロフィール
教育活動
研究活動
社会活動
リサーチマップ・
Jグローバル
KAKEN
注目研究

研究者総覧で最新データを確認する

2024年11月15日更新

職名: 准教授
電話: 088-633-9225
電子メール: sakane@tokushima-u.ac.jp
学歴: 2006/3: 徳島大学大学院医学研究科プロテオミクス医科学専攻博士課程修了
2008/3: 徳島大学医学部医学科卒業
学位: 博士(医学) (徳島大学) (2006年3月)
職歴・経歴: 2008/4: 徳島大学助教, 大学院ヘルスバイオサイエンス研究部 (-2015.3.)
2015/4: 徳島大学助教, 大学院医歯薬学研究部 (-2017.3.)
2017/4: 徳島大学准教授, 大学院医歯薬学研究部

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11月15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)
技術英語入門 (学部)
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11月15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: 細胞内小胞輸送ならびに細胞骨格の制御機構に関する研究 (細胞内シグナル伝達, 神経伝達物質放出, 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)

論文

Shogo Miyamura, Ryo Oe, Takuya Nakahara, Hidenori Koresawa, Shota Okada, Shuji Taue, Yu Tokizane, Takeo Minamikawa, Kunihiro Otsuka, Ayuko Sakane, Takuya Sasaki, Koji Yasutomo, Taira Kajisa and Takeshi Yasui :
Rapid, high-sensitivity detection of biomolecules using dual-comb biosensing,
Scientific Reports, Vol.13, 14541, 2023.

(要約): Rapid, sensitive detection of biomolecules is important for biosensing of infectious pathogens as well as biomarkers and pollutants. For example, biosensing of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is still strongly required for the fight against coronavirus disease 2019 (COVID-19) pandemic. Here, we aim to achieve the rapid and sensitive detection of SARS-CoV-2 nucleocapsid protein antigen by enhancing the performance of optical biosensing based on optical frequency combs (OFC). The virus-concentration-dependent optical spectrum shift produced by antigen-antibody interactions is transformed into a photonic radio-frequency (RF) shift by a frequency conversion between the optical and RF regions in the OFC, facilitating rapid and sensitive detection with well-established electrical frequency measurements. Furthermore, active-dummy temperature-drift compensation with a dual-comb configuration enables the very small change in the virus-concentration-dependent signal to be extracted from the large, variable background signal caused by temperature disturbance. The achieved performance of dual-comb biosensing will greatly enhance the applicability of biosensors to viruses, biomarkers, environmental hormones, and so on.
(キーワード): Humans / COVID-19 / SARS-CoV-2 / COVID-19 Testing / Biosensing Techniques / Viruses / Antigens, Viral
(出版サイトへのリンク): ● Publication site (DOI): 10.1038/s41598-023-41436-3
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 37752134; ● Search Scopus @ Elsevier (PMID): 37752134; ● Search Scopus @ Elsevier (DOI): 10.1038/s41598-023-41436-3

(DOI: 10.1038/s41598-023-41436-3, PubMed: 37752134) Tomohiko Maruo, Kiyohito Mizutani, Muneaki Miyata, Toshihiko Kuriu, Shotaro Sakakibara, Hatena Takahashi, Daichi Kida, Kouki Maesaka, Tsukiko Sugaya, Ayuko Sakane, Takuya Sasaki, Yoshimi Takai and Kenji Mandai :
s-Afadin binds to MAGUIN/Cnksr2 and regulates the localization of the AMPA receptor and glutamatergic synaptic response in hippocampal neurons.,
The Journal of Biological Chemistry, Vol.299, No.4, 2023.

(要約): A hippocampal mossy fiber synapse implicated in learning and memory is a complex structure in which a presynaptic bouton attaches to the dendritic trunk by puncta adherentia junctions (PAJs) and wraps multiply branched spines. The postsynaptic densities (PSDs) are localized at the heads of each of these spines and faces to the presynaptic active zones. We previously showed that the scaffolding protein afadin regulates the formation of the PAJs, PSDs, and active zones in the mossy fiber synapse. Afadin has two splice variants: l-afadin and s-afadin. l-Afadin, but not s-afadin, regulates the formation of the PAJs but the roles of s-afadin in synaptogenesis remain unknown. We found here that s-afadin more preferentially bound to MAGUIN (a product of the Cnksr2 gene) than l-afadin in vivo and in vitro. MAGUIN/CNKSR2 is one of the causative genes for nonsyndromic X-linked intellectual disability accompanied by epilepsy and aphasia. Genetic ablation of MAGUIN impaired PSD-95 localization and α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic (AMPA) receptor surface accumulation in cultured hippocampal neurons. Our electrophysiological analysis revealed that the postsynaptic response to glutamate, but not its release from the presynapse, was impaired in the MAGUIN-deficient cultured hippocampal neurons. Furthermore, disruption of MAGUIN did not increase the seizure susceptibility to flurothyl, a GABAA receptor antagonist. These results indicate that s-afadin binds to MAGUIN and regulates the PSD-95-dependent cell surface localization of the AMPA receptor and glutamatergic synaptic responses in the hippocampal neurons and that MAGUIN is not involved in the induction of epileptic seizure by flurothyl in our mouse model.
(キーワード): AMPA receptor / electrophysiology / epilepsy / scaffold protein / シナプス (synapse)
(出版サイトへのリンク): ● Publication site (DOI): 10.1016/j.jbc.2023.103040
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 36803960; ● Search Scopus @ Elsevier (PMID): 36803960; ● Search Scopus @ Elsevier (DOI): 10.1016/j.jbc.2023.103040

(DOI: 10.1016/j.jbc.2023.103040, PubMed: 36803960) 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) 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) 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) 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) 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) 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)

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. 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. 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.

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. 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. 坂根亜由子 :
1分子の構造変化から観た細胞運動の制御機構,
第6回生命科学阿波踊りシンポジウム, 2015年8月. 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. 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. 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. 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. 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. 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, 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, 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.

研究会・報告書: 坂根亜由子 :
細胞接着形成を制御する細胞内小胞輸送とアクチン細胞骨格系のクロストーク機構,
第3回生命科学阿波踊りシンポジウム, 2011年8月. 坂根亜由子 :
細胞の形作りの分子機構の研究からがん転移・浸潤の病態を探る,
HBS 5教育部第20回月例交流セミナー, 2011年5月.

特許: 研究者総覧に該当データはありませんでした。
作品: 研究者総覧に該当データはありませんでした。
補助金・競争的資金: 光コムの医光融合研究に立脚した新興・再興ウイルスの超高感度・迅速検出 (研究課題/領域番号: 22H00303 )
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 )
集団的細胞運動を制御するJRABの構造変化の階層的解析-情報から生体に至るまで- (研究課題/領域番号: 17K08636 )
小胞輸送とアクチン細胞骨格再編成から観る脳の高次構造・機能構築のダイナミズム (研究課題/領域番号: 26460370 )
集団的細胞運動を支える細胞内小胞輸送とアクチン細胞骨格再編成のクロストーク制御 (研究課題/領域番号: 25111723 )
高次生命機能システムを支えるエキソサイトーシスのしくみ (研究課題/領域番号: 24790285 )
高次神経機能を支えるシナプス形成・成熟過程と小胞輸送 (研究課題/領域番号: 22790293 )
シナプス形成・成熟過程を支える小胞輸送の制御機構 (研究課題/領域番号: 20890149 )
研究者番号（60509777）による検索

その他: 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11月15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)
所属学会・所属協会: 日本生化学会
日本分子生物学会
日本細胞生物学会
日本癌学会
社団法人日本内分泌学会
委員歴・役員歴: 研究者総覧に該当データはありませんでした。
受賞: 2007年4月, 財団法人大塚芳満記念財団助成金 (財団法人大塚芳満記念財団)
2007年12月, 第24回井上研究奨励賞 (財団法人井上科学振興財団)
2007年12月, 第6回徳島新聞医学研究助成金 (財団法人徳島新聞社会文化事業団)
2010年3月, 平成21年度岡奨学賞 (徳島大学)
平成26年度「徳島大学若手研究者学長表彰」 (徳島大学)
活動: 研究者総覧に該当データはありませんでした。

リサーチマップで最新データを確認するＪグローバルで最新データを確認する

2024年11月10日更新

2024年11月9日更新

Ｊグローバル

Jグローバル最終確認日: 2024/11/9 01:21
氏名（漢字）: 坂根亜由子
氏名（フリガナ）: JグローバルAPIで取得できませんでした。
氏名（英字）: Sakane Ayuko
所属機関: 徳島大学准教授
徳島大学ポストLEDフォトニクス研究所(pLED) 准教授(兼任)

リサーチマップ

researchmap最終確認日: 2024/11/10 01:34
氏名（漢字）: 坂根亜由子
氏名（フリガナ）: リサーチマップAPIで取得できませんでした。
氏名（英字）: Sakane Ayuko
プロフィール: リサーチマップAPIで取得できませんでした。
登録日時: 2018/11/15 20:35
更新日時: 2024/10/2 13:05
アバター画像URI: リサーチマップAPIで取得できませんでした。
ハンドル: リサーチマップAPIで取得できませんでした。
eメール: リサーチマップAPIで取得できませんでした。
eメール（その他）: リサーチマップAPIで取得できませんでした。
携帯メール: リサーチマップAPIで取得できませんでした。
性別: リサーチマップAPIで取得できませんでした。
没年月日: リサーチマップAPIで取得できませんでした。
所属ID: 0344000000
所属: 徳島大学
部署: 大学院医歯薬学研究部
職名: 准教授
学位: 医学博士
学位授与機関: 徳島大学
URL: リサーチマップAPIで取得できませんでした。
科研費研究者番号: リサーチマップAPIで取得できませんでした。
Google Analytics ID: リサーチマップAPIで取得できませんでした。
ORCID ID: リサーチマップAPIで取得できませんでした。
その他の所属ID: リサーチマップAPIで取得できませんでした。
その他の所属名: リサーチマップAPIで取得できませんでした。
その他の所属部署: リサーチマップAPIで取得できませんでした。
その他の所属職名: リサーチマップAPIで取得できませんでした。
最近のエントリー: リサーチマップAPIで取得できませんでした。
Read会員ID: リサーチマップAPIで取得できませんでした。
経歴
受賞
Misc
論文
講演・口頭発表等
書籍等出版物
研究キーワード: リサーチマップAPIで取得できませんでした。
研究分野
所属学協会
担当経験のある科目: リサーチマップAPIで取得できませんでした。
その他: リサーチマップAPIで取得できませんでした。
Works: リサーチマップAPIで取得できませんでした。
特許: リサーチマップAPIで取得できませんでした。
学歴
委員歴: リサーチマップAPIで取得できませんでした。
社会貢献活動: リサーチマップAPIで取得できませんでした。

ＫＡＫＥＮで最新データを確認する

2024年11月9日更新

研究者番号: 60509777

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

所属（過去の研究課題 情報に基づく）*注記: 2021/4/1 – 2024/4/1 : 徳島大学, 大学院医歯薬学研究部(医学域), 准教授
2018/4/1 – 2019/4/1 : 徳島大学, 大学院医歯薬学研究部(医学域), 准教授
2017/4/1 : 徳島大学, 大学院医歯薬学研究部(医学系), 准教授
2016/4/1 : 徳島大学, 大学院医歯薬学研究部(医学系), 助教
2015/4/1 : 徳島大学, 大学院医歯薬学研究部, 助教
2012/4/1 – 2014/4/1 : 徳島大学, ヘルスバイオサイエンス研究部, 助教
2008/4/1 – 2011/4/1 : 徳島大学, 大学院・ヘルスバイオサイエンス研究部, 助教

審査区分/研究分野

研究代表者

生物系 / 医歯薬学 / 基礎医学 / 医化学一般
生物系
小区分48040:医化学関連

研究代表者以外

中区分30:応用物理工学およびその関連分野

キーワード

研究代表者

高次神経機能 / シナプス形成 / シナプス成熟 / 小胞輸送 / Rabファミリー低分子量G蛋白質 / シナプス形戌 / 脳・神経系形成 / 高次神経機能獲得 / シナプス形成・成熟 / 脳・神経系 / 高次生命機能システム / エキソサイトーシス / 細胞間接着形成 / 神経突起伸長・シナプス形成 / 集団的細胞運動 / アクチン細胞骨格 / 細胞内小胞輸送 / Rab13-JRAB系 / 脳の高次構造・機能 / アクチン細胞骨格の再編成 / JRAB / 1分子構造変化 / 蛋白質間相互作用 / 階層的解析 / JRAB １分子構造変化 / １分子構造変化 / 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

研究代表者以外

光コム / マイクロ光コム / バイオセンサー / 新型コロナウイルス

研究課題研究成果共同研究者

「研究課題をさがす」で表示
テキスト（CSV）で出力

テキスト（CSV）で出力

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

研究者を探す

坂根 亜由子

Ｊグローバル

リサーチマップ

研究代表者

研究代表者以外

研究代表者

研究代表者以外

坂根亜由子