Structural basis for cofilin binding and actin filament disassembly

Kotaro Tanaka, Shuichi Takeda, Kaoru Mitsuoka, Toshiro Oda, Chieko Kimura-Sakiyama, Yuichiro Maéda and Akihiro Narita ()
Additional contact information
Kotaro Tanaka: Nagoya University
Shuichi Takeda: Nagoya University
Kaoru Mitsuoka: Osaka University
Toshiro Oda: Tokai Gakuin University
Chieko Kimura-Sakiyama: Nagoya University
Yuichiro Maéda: Nagoya University
Akihiro Narita: Nagoya University

Nature Communications, 2018, vol. 9, issue 1, 1-12

Abstract: Abstract 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.

Date: 2018
References: Add references at CitEc
Citations:

Downloads: (external link)
https://www.nature.com/articles/s41467-018-04290-w Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:9:y:2018:i:1:d:10.1038_s41467-018-04290-w

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/s41467-018-04290-w

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().