The role of the FH1 domain and profilin in formin-mediated actin-filament elongation and nucleation.

ABSTRACT:

Background

Formin proteins nucleate actin filaments de novo and stay associated with the growing barbed end. Whereas the formin-homology (FH) 2 domains mediate processive association, the FH1 domains-in concert with the actin-monomer-binding protein profilin-increase the rate of barbed-end elongation. The mechanism by which this effect is achieved is not well understood.

Results

We used total internal reflection fluorescence microscopy to measure the effect of profilin on the elongation of single actin filaments associated with FH1FH2 constructs (derived from the formin Bni1p from S. cerevisiae) with FH1 domains containing one to eight profilin-binding polyproline tracks. Over a large range of profilin concentrations (0.5-25 microM), the rate of barbed-end elongation increas

SUBMITTER: Paul AS 

PROVIDER: S-EPMC3712528 | biostudies-literature | 2008 Jan

REPOSITORIES: biostudies-literature