Structural basis for cofilin binding and actin filament disassembly

Nature Communications
Kotaro TanakaAkihiro Narita

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.

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Methods Mentioned

BETA
light microscopy
gel filtration

Software Mentioned

Gctf
_ space _ refine
COOT
NAMD
DynDom
real
e2helixboxer
RELION
MDFF
phenix

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