GMF severs actin-Arp2/3 complex branch junctions by a cofilin-like mechanism.

ABSTRACT:

Background

Branched actin filament networks driving cell motility, endocytosis, and intracellular transport are assembled in seconds by the Arp2/3 complex and must be equally rapidly debranched and turned over. One of the only factors known to promote debranching of actin networks is the yeast homolog of glia maturation factor (GMF), which is structurally related to the actin filament-severing protein cofilin. However, the identity of the molecular mechanism underlying debranching and whether this activity extends to mammalian GMF have remained open questions.

Results

Using scanning mutagenesis and total internal reflection fluorescence microscopy, we show that GMF depends on two separate surfaces for debranching. One is analogous to the G-actin and F-actin binding site on c

SUBMITTER: Ydenberg CA 

PROVIDER: S-EPMC3714218 | biostudies-literature | 2013 Jun

REPOSITORIES: biostudies-literature