論文

査読有り 筆頭著者 国際誌
2018年5月

Structural basis for cofilin binding and actin filament disassembly

Nature Communications
  • Kotaro Tanaka
  • ,
  • Shuichi Takeda
  • ,
  • Kaoru Mitsuoka
  • ,
  • Toshiro Oda
  • ,
  • Chieko Kimura-Sakiyama
  • ,
  • Yuichiro Maéda
  • ,
  • Akihiro Narita

9
1
開始ページ
1860
終了ページ
1860
記述言語
英語
掲載種別
研究論文(学術雑誌)
DOI
10.1038/s41467-018-04290-w
出版者・発行元
Springer Science and Business Media LLC

Actin depolymerizing factor (ADF) and cofilin accelerate actin dynamics by severing and disassembling actin filaments. Here, we present the 3.8 Å resolution cryo-EM structure of cofilactin (cofilin-decorated actin filament). The actin subunit structure of cofilactin (C-form) is distinct from those of F-actin (F-form) and monomeric actin (G-form). During the transition between these three conformations, the inner domain of actin (subdomains 3 and 4) and the majority of subdomain 1 move as two separate rigid bodies. The cofilin-actin interface consists of three distinct parts. Based on the rigid body movements of actin and the three cofilin-actin interfaces, we propose models for the cooperative binding of cofilin to actin, preferential binding of cofilin to ADP-bound actin filaments and cofilin-mediated severing of actin filaments.

リンク情報
DOI
https://doi.org/10.1038/s41467-018-04290-w
PubMed
https://www.ncbi.nlm.nih.gov/pubmed/29749375
PubMed Central
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5945598
URL
http://www.nature.com/articles/s41467-018-04290-w.pdf
URL
http://www.nature.com/articles/s41467-018-04290-w
ID情報
  • DOI : 10.1038/s41467-018-04290-w
  • eISSN : 2041-1723
  • PubMed ID : 29749375
  • PubMed Central 記事ID : PMC5945598

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