Developmental cell · 2015
An Engineered Minimal WASP-Myosin Fusion Protein Reveals Essential Functions for Endocytosis.
СтатьяПоддержка NIH: внешняя программаVideo-Audio MediaНазвание и аннотация: Перевод пока не подготовлен
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Lewellyn Eric B, Pedersen Ross T A, Hong Jessica, Lu Rebecca, Morrison Huntly M, Drubin David G
Аннотация
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 is essential for allowing actin polymerization to drive membrane invagination.