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アイテム

  1. 研究者名(五十音順)
  2. 徳樂 清孝(TOKURAKU Kiyotaka)
  1. 学術雑誌論文

Actin-binding domain of Rng2 sparsely bound on F-actin strongly inhibits actin movement on myosin II

http://hdl.handle.net/10258/0002000103
http://hdl.handle.net/10258/0002000103
8603f974-6c6f-40b9-bcb1-f1e464814d30
名前 / ファイル ライセンス アクション
e202201469.full.pdf e202201469.full.pdf (3 MB)
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アイテムタイプ 学術雑誌論文 / Journal Article.(1)
公開日 2023-10-24
書誌情報 en : Life Science Alliance

巻 6, 号 1, ページ数 18, 発行日 2023
タイトル
タイトル Actin-binding domain of Rng2 sparsely bound on F-actin strongly inhibits actin movement on myosin II
言語 en
言語
言語 eng
資源タイプ
資源タイプ識別子 http://purl.org/coar/resource_type/c_6501
資源タイプ journal article
アクセス権
アクセス権 open access
アクセス権URI http://purl.org/coar/access_right/c_abf2
著者 Hayakawa, Yuuki

× Hayakawa, Yuuki

en Hayakawa, Yuuki

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Takaine, Masak

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en Takaine, Masak

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Ngo, Kien Xuan

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en Ngo, Kien Xuan

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Imai, Taiga

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en Imai, Taiga

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Yamada, Masafumi D

× Yamada, Masafumi D

en Yamada, Masafumi D

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Behjat, Arash Badami

× Behjat, Arash Badami

en Behjat, Arash Badami

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Umeda, Kenichi

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en Umeda, Kenichi

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Hirose, Keiko

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en Hirose, Keiko

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Yurtsever, Ayhan

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en Yurtsever, Ayhan

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Kodera, Noriyuki

× Kodera, Noriyuki

en Kodera, Noriyuki

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徳楽, 清孝

× 徳楽, 清孝

en Tokuraku, Kiyotaka

ja 徳楽, 清孝

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Numata, Osamu

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en Numata, Osamu

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Fukuma, Takeshi

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en Fukuma, Takeshi

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Ando, Toshio

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Nakano, Kentaro

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Uyeda, Taro QP

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en Uyeda, Taro QP

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抄録
内容記述タイプ Abstract
内容記述 We report a case in which sub-stoichiometric binding of an actin-binding protein has profound structural and functional consequences, providing an insight into the fundamental properties of actin regulation. Rng2 is an IQGAP contained in contractile rings in the fission yeast Schizosaccharomyces pombe. Here, we used high-speed atomic force microscopy and electron microscopy and found that sub-stoichiometric binding of the calponin-homology actin-binding domain of Rng2 (Rng2CHD) induces global structural changes in skeletal muscle actin filaments, including shortening of the filament helical pitch. Sub-stoichiometric binding of Rng2CHD also reduced the affinity between actin filaments and muscle myosin II carrying ADP and strongly inhibited the motility of actin filaments on myosin II in vitro. On skeletal muscle myosin II–coated surfaces, Rng2CHD stopped the actin movements at a binding ratio of 11%. Rng2CHD also inhibited actin movements on myosin II of the amoeba Dictyostelium, but in this case, by detaching actin filaments from myosin II–coated surfaces. Thus, sparsely bound Rng2CHD induces apparently cooperative structural changes in actin filaments and inhibits force generation by actomyosin II.
言語 en
出版者
出版者 Life Science Alliance LLC
言語 en
DOI
関連タイプ isIdenticalTo
識別子タイプ DOI
関連識別子 10.26508/lsa.202201469
ISSN
収録物識別子タイプ EISSN
収録物識別子 2575-1077
権利
権利情報 © 2022 Hayakawa et al.
言語 en
著者版フラグ
出版タイプ VoR
出版タイプResource http://purl.org/coar/version/c_970fb48d4fbd8a85
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