Structural basis for cofilin binding and actin filament disassembly

被引：118

作者：

Tanaka, Kotaro ^{[1
]}

Takeda, Shuichi ^{[1
]}

Mitsuoka, Kaoru ^{[2
]}

Oda, Toshiro ^{[3
]}

Kimura-Sakiyama, Chieko ^{[1
,5
]}

Maeda, Yuichiro ^{[1
,4
]}

Narita, Akihiro ^{[1
]}

机构：

[1] Nagoya Univ, Grad Sch Sci, Struct Biol Res Ctr, Chikusa Ku, Furo Cho, Nagoya, Aichi 4648601, Japan

[2] Osaka Univ, Res Ctr Ultra High Voltage Electron Microscopy, 7-1 Mihogaoka, Ibaraki, Osaka 5670047, Japan

[3] Tokai Gakuin Univ, Fac Hlth & Welf, Nakakirino Cyo 5-68, Gifu 5048511, Japan

[4] Toyota Phys & Chem Res Inst, 41-1 Yokomichi, Nagakute, Aichi 4801192, Japan

[5] Doshisha Univ, Fac Life & Med Sci, Dept Med Life Syst, 1-3 Miyakodani, Kyoto 6100394, Japan

来源：

NATURE COMMUNICATIONS | 2018年 / 9卷

关键词：

CRYO-EM STRUCTURE; DEPOLYMERIZING FACTOR; PHOSPHOINOSITIDE-BINDING; ADF/COFILIN; DYNAMICS; MUSCLE; FLEXIBILITY; COMPLEX; PROTEIN; POLYMERIZATION;

D O I：

10.1038/s41467-018-04290-w

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

Actin depolymerizing factor (ADF) and cofilin accelerate actin dynamics by severing and disassembling actin filaments. Here, we present the 3.8 A 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.

引用

页数：12

共 65 条

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