An Engineered Minimal WASP-Myosin Fusion Protein Reveals Essential Functions for Endocytosis.

ABSTRACT: Actin polymerization powers membrane deformation during many processes, including clathrin-mediated endocytosis (CME). During CME in yeast, actin polymerization is triggered and coordinated by a six-protein WASP/Myosin complex that includes WASP, class I myosins (Myo3 and Myo5), WIP (Vrp1), and two other proteins. We show that a single engineered protein can replace this entire complex while still supporting CME. This engineered protein reveals that the WASP/Myosin complex has four essential activities: recruitment to endocytic sites, anchorage to the plasma membrane, Arp2/3 activation, and transient actin filament binding by the motor domain. The requirement for both membrane and F-actin binding reveals that myosin-mediated coupling between actin filaments and the base of endocytic sites

SUBMITTER: Lewellyn EB 

PROVIDER: S-EPMC4643393 | biostudies-literature | 2015 Nov

REPOSITORIES: biostudies-literature