Coordination of the filament stabilizing versus destabilizing activities of cofilin through its secondary binding site on actin.

ABSTRACT: Cofilin is a ubiquitous modulator of actin cytoskeleton dynamics that can both stabilize and destabilize actin filaments depending on its concentration and/or the presence of regulatory co-factors. Three charge-reversal mutants of yeast cofilin, located in cofilin's filament-specific secondary binding site, were characterized in order to understand why disruption of this site leads to enhanced filament disassembly. Crystal structures of the mutants showed that the mutations specifically affect the secondary actin-binding interface, leaving the primary binding site unaltered. The mutant cofilins show enhanced activity compared to wild-type cofilin in severing and disassembling actin filaments. Electron microscopy and image analysis revealed long actin filaments in the presence of wild-type

SUBMITTER: Aggeli D 

PROVIDER: S-EPMC4241054 | biostudies-literature | 2014 Jun

REPOSITORIES: biostudies-literature