| Item type |
学術雑誌論文 / Journal Article.(1) |
| 公開日 |
2017-07-28 |
| 書誌情報 |
en : Scientific Reports
巻 6,
p. 35449,
発行日 2016-10-20
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| タイトル |
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タイトル |
Allosteric regulation by cooperative conformational changes of actin filaments drives mutually exclusive binding with cofilin and myosin |
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言語 |
en |
| 言語 |
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言語 |
eng |
| 資源タイプ |
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資源タイプ識別子 |
http://purl.org/coar/resource_type/c_6501 |
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資源タイプ |
journal article |
| アクセス権 |
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アクセス権 |
open access |
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アクセス権URI |
http://purl.org/coar/access_right/c_abf2 |
| 著者 |
NGO, Kien Xuan
UMEKI, Nobuhisa
貴嶋, 紗久
KODERA, Noriyuki
上野, 寛朗
FURUTANI-UMEZU, Nozomi
NAKAJIMA, Jun
NOGUCHI, Taro Q. P.
NAGASAKI, Akira
徳樂, 清孝
UYEDA, Taro Q. P.
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| 室蘭工業大学研究者データベースへのリンク |
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徳樂 清孝（TOKURAKU Kiyotaka） |
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http://rdsoran.muroran-it.ac.jp/html/100000137_ja.html |
| 抄録 |
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内容記述タイプ |
Abstract |
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内容記述 |
Heavy meromyosin (HMM) of myosin II and cofilin each binds to actin filaments cooperatively and forms clusters along the filaments, but it is unknown whether the two cooperative bindings are correlated and what physiological roles they have. Fluorescence microscopy demonstrated that HMM-GFP and cofilin-mCherry each bound cooperatively to different parts of actin filaments when they were added simultaneously in 0.2 μM ATP, indicating that the two cooperative bindings are mutually exclusive. In 0.1 mM ATP, the motor domain of myosin (S1) strongly inhibited the formation of cofilin clusters along actin filaments. Under this condition, most actin protomers were unoccupied by S1 at any given moment, suggesting that transiently bound S1 alters the structure of actin filaments cooperatively and/or persistently to inhibit cofilin binding. Consistently, cosedimentation experiments using copolymers of actin and actin-S1 fusion protein demonstrated that the fusion protein affects the neighboring actin protomers, reducing their affinity for cofilin. In reciprocal experiments, cofilin-actin fusion protein reduced the affinity of neighboring actin protomers for S1. Thus, allosteric regulation by cooperative conformational changes of actin filaments contributes to mutually exclusive cooperative binding of myosin II and cofilin to actin filaments, and presumably to the differential localization of both proteins in cells. |
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言語 |
en |
| 出版者 |
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出版者 |
SPRINGER NATURE |
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言語 |
en |
| 出版者版へのリンク |
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10.1038/srep35449 |
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https://dx.doi.org/10.1038/srep35449 |
| DOI |
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関連タイプ |
isIdenticalTo |
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識別子タイプ |
DOI |
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関連識別子 |
10.1038/srep35449 |
| 日本十進分類法 |
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主題Scheme |
NDC |
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主題 |
464 |
| ISSN |
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収録物識別子タイプ |
PISSN |
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収録物識別子 |
2045-2322 |
| 権利 |
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言語 |
ja |
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権利情報 |
©NGO et.al. 2016 This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ |
| 著者版フラグ |
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出版タイプ |
VoR |
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出版タイプResource |
http://purl.org/coar/version/c_970fb48d4fbd8a85 |
| フォーマット |
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内容記述タイプ |
Other |
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内容記述 |
application/pdf |
srep_6_35449 (2.3 MB)
