Structure and activity of full-length formin mDia1.

ABSTRACT: Formins are a conserved family of actin assembly-promoting factors with essential and diverse biological roles. Most of our biochemical understanding of formin effects on actin dynamics is derived from studies using formin fragments. In addition, all structural information on formins has been limited to fragments. This has left open key questions about the structure, activity and regulation of intact formin proteins. Here, we isolated full-length mouse mDia1 (mDia1-FL) and found that it forms tightly autoinhibited dimers that can only be partially activated by RhoA. We solved the structure of autoinhibited mDia1-FL using electron microscopy and single particle analysis. Docking of crystal structures into the three dimensional reconstruction revealed that the fork-shaped N-terminal diaphano

SUBMITTER: Maiti S 

PROVIDER: S-EPMC3416746 | biostudies-literature | 2012 Jun

REPOSITORIES: biostudies-literature