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Type-I myosins promote actin polymerization to drive membrane bending in endocytosis

By Hetty E. Manenschijn, Andrea Picco, Markus Mund, Jonas Ries, Marko Kaksonen

Posted 09 Dec 2018
bioRxiv DOI: 10.1101/490011 (published DOI: 10.7554/eLife.44215)

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.

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