『徳島大学 教育・研究者情報データベース (EDB)』---[学外] /
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EID=355247EID:355247, Map:0, LastModified:2019年8月28日(水) 19:31:12, Operator:[大家 隆弘], Avail:TRUE, Censor:承認済, Owner:[米村 重信], Read:継承, Write:継承, Delete:継承.
種別 (必須): 学術論文 (審査論文) [継承]
言語 (必須): 英語 [継承]
招待 (推奨):
審査 (推奨): Peer Review [継承]
カテゴリ (推奨):
共著種別 (推奨): 国際共著 (徳島大学内研究者と国外研究機関所属研究者との共同研究) [継承]
学究種別 (推奨):
組織 (推奨):
著者 (必須): 1. (英) Maki koichiro (日) 牧 功一郎 (読)
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2. (英) Han Sung-Woong (日) (読)
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3. (英) Hirano Yoshinori (日) (読)
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4.米村 重信 ([徳島大学.大学院医歯薬学研究部.医学域.医科学部門.生理系.細胞生物学])
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5. (英) Takoshima Toshio (日) 箱嶋 敏夫 (読)
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6. (英) Adachi Taiji (日) 安達 泰治 (読)
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題名 (必須): (英) Real-time TIRF observation of vinculin recruitment to stretched alpha-catenin by AFM  (日)    [継承]
副題 (任意):
要約 (任意): (英) Adherens junctions (AJs) adaptively change their intensities in response to intercellular tension; therefore, they integrate tension generated by individual cells to drive multicellular dynamics, such as morphogenetic change in embryos. Under intercellular tension, α-catenin, which is a component protein of AJs, acts as a mechano-chemical transducer to recruit vinculin to promote actin remodeling. Although in vivo and in vitro studies have suggested that α-catenin-mediated mechanotransduction is a dynamic molecular process, which involves a conformational change of α-catenin under tension to expose a cryptic vinculin binding site, there are no suitable experimental methods to directly explore the process. Therefore, in this study, we developed a novel system by combining atomic force microscopy (AFM) and total internal reflection fluorescence (TIRF). In this system, α-catenin molecules (residues 276-634; the mechano-sensitive M-M domain), modified on coverslips, were stretched by AFM and their recruitment of Alexa-labeled full-length vinculin molecules, dissolved in solution, were observed simultaneously, in real time, using TIRF. We applied a physiologically possible range of tensions and extensions to α-catenin and directly observed its vinculin recruitment. Our new system could be used in the fields of mechanobiology and biophysics to explore functions of proteins under tension by coupling biomechanical and biochemical information.  (日)    [継承]
キーワード (推奨): 1. (英) Animals (日) (読) [継承]
2. (英) Fluorometry (日) (読) [継承]
3. (英) Mice (日) (読) [継承]
4. (英) Microscopy, Atomic Force (日) (読) [継承]
5. (英) Protein Binding (日) (読) [継承]
6. (英) Vinculin (日) (読) [継承]
7. (英) alpha Catenin (日) (読) [継承]
発行所 (推奨):
誌名 (必須): Scientific Reports ([Nature Publishing Group])
(eISSN: 2045-2322)

ISSN (任意): 2045-2322
ISSN: 2045-2322 (eISSN: 2045-2322)
Title: Scientific reports
Title(ISO): Sci Rep
Publisher: Nature Portfolio
 (NLM Catalog  (Scopus  (CrossRef (Scopus information is found. [need login])
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(必須): 8 [継承]
(必須): 1 [継承]
(必須): 1575 1575 [継承]
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年月日 (必須): 西暦 2018年 1月 25日 (平成 30年 1月 25日) [継承]
URL (任意):
DOI (任意): 10.1038/s41598-018-20115-8    (→Scopusで検索) [継承]
PMID (任意): 29371682    (→Scopusで検索) [継承]
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備考 (任意): 1.(英) Article.ELocationID: 10.1038/s41598-018-20115-8  (日)    [継承]
2.(英) Article.PublicationTypeList.PublicationType: Journal Article  (日)    [継承]
3.(英) Article.PublicationTypeList.PublicationType: Research Support, Non-U.S. Gov't  (日)    [継承]

標準的な表示

和文冊子 ● koichiro Maki, Sung-Woong Han, Yoshinori Hirano, Shigenobu Yonemura, Toshio Takoshima and Taiji Adachi : Real-time TIRF observation of vinculin recruitment to stretched alpha-catenin by AFM, Scientific Reports, Vol.8, No.1, 1575, 2018.
欧文冊子 ● koichiro Maki, Sung-Woong Han, Yoshinori Hirano, Shigenobu Yonemura, Toshio Takoshima and Taiji Adachi : Real-time TIRF observation of vinculin recruitment to stretched alpha-catenin by AFM, Scientific Reports, Vol.8, No.1, 1575, 2018.

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