RT Journal Article
SR Electronic
T1 Type-I myosins promote actin polymerization to drive membrane bending in endocytosis
JF bioRxiv
FD Cold Spring Harbor Laboratory
SP 490011
DO 10.1101/490011
A1 Hetty E. Manenschijn
A1 Andrea Picco
A1 Markus Mund
A1 Jonas Ries
A1 Marko Kaksonen
YR 2018
UL http://biorxiv.org/content/early/2018/12/09/490011.abstract
AB Clathrin-mediated endocytosis in budding yeast requires the formation of a dynamic actin network that produces the force to invaginate the plasma membrane against the intracellular turgor pressure. The type-I myosins Myo3 and Myo5 are important for endocytic membrane reshaping, but mechanistic details of their function remain scarce. Here, we studied the function of Myo3 and Myo5 during endocytosis using quantitative live-cell imaging and genetic perturbations. We show that the type-I myosins promote, in a dose-dependent way, the growth and expansion of the actin network, which controls the speed of membrane and coat internalization. We found that this myosin-activity is independent of the actin nucleation promoting activity of myosins, and cannot be compensated for by increasing actin nucleation. Our results suggest a new mechanism for type-I myosins to produce force by promoting actin filament polymerization.