Cofilin tunes the nucleotide state of actin filaments and severs at bare and decorated segment boundaries.

ABSTRACT: Actin-based motility demands the spatial and temporal coordination of numerous regulatory actin-binding proteins (ABPs), many of which bind with affinities that depend on the nucleotide state of actin filament. Cofilin, one of three ABPs that precisely choreograph actin assembly and organization into comet tails that drive motility in vitro, binds and stochastically severs aged ADP actin filament segments of de novo growing actin filaments. Deficiencies in methodologies to track in real time the nucleotide state of actin filaments, as well as cofilin severing, limit the molecular understanding of coupling between actin filament chemical and mechanical states and severing. We engineered a fluorescently labeled cofilin that retains actin filament binding and severing activities. Because cofi

SUBMITTER: Suarez C 

PROVIDER: S-EPMC3100394 | biostudies-literature | 2011 May

REPOSITORIES: biostudies-literature