Multiple Conformations of F-actin

Toshiro Oda; Yuichiro Maéda

doi:10.1016/j.str.2010.05.009

Multiple Conformations of F-actin

Structure. 2010 Jul 14;18(7):761-7. doi: 10.1016/j.str.2010.05.009.

Authors

Toshiro Oda¹, Yuichiro Maéda

Affiliation

¹ X-ray Structural Analysis Team, RIKEN SPring-8 Center, RIKEN Harima Institute 1-1-1 Kouto, Sayo-gun, Hogo, Japan. toda@spring8.or.jp

PMID: 20637412
DOI: 10.1016/j.str.2010.05.009

Abstract

Actin works within eukaryotic cells to facilitate a variety of cellular processes, which are driven by the assembly of G-actin (monomeric form) into F-actin (fibrous form), and the disassembly of F-actin into G-actin. F-actin adopts multiple conformations, which are specified by interactions with various actin-binding proteins. Knowledge of the multiple conformations of actin is the key for understanding its cellular functions. Recently, we published a refined model for F-actin. In this review, based on this model, we discuss the origin, mechanism, and possible physiological significance of the multiple conformations of F-actin.

Publication types

Review

MeSH terms

Actins / chemistry*
Actins / physiology*
Models, Molecular*
Protein Binding
Protein Conformation*
Thermodynamics

Substances

Actins