Common formin-regulating sequences in Smy1 and Bud14 are required for the control of actin cable assembly in vivo.

ABSTRACT: Formins comprise a large family of proteins with diverse roles in remodeling the actin cytoskeleton. However, the spatiotemporal mechanisms used by cells to control formin activities are only beginning to be understood. Here we dissected Smy1, which has dual roles in regulating formins and myosin. Using mutagenesis, we identified specific sequences in Smy1 critical for its in vitro inhibitory effects on the FH2 domain of the formin Bnr1. By integrating smy1 alleles targeting those sequences, we genetically uncoupled Smy1's functions in regulating formins and myosin. Quantitative imaging analysis further demonstrated that the ability of Smy1 to directly control Bnr1 activity is crucial in vivo for proper actin cable length, shape, and velocity and, in turn, efficient secretory vesicle trans

SUBMITTER: Eskin JA 

PROVIDER: S-EPMC4803308 | biostudies-literature | 2016 Mar

REPOSITORIES: biostudies-literature