Why the study?
Type-I myosins Myo3 and Myo5 are important for endocytic membrane reshaping in budding yeast, but mechanistic details of their function remain scarce.
Type-I myosins Myo3 and Myo5 promote actin filament polymerization to drive membrane bending during clathrin-mediated endocytosis in yeast, independent of their actin nucleation promoting activity.
Myosins promote actin growth to speed yeast endocytosis independent of NPF activity; extends models of force generation but leaves open mammalian relevance.
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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Manenschijn et al. (2018) studied this question.
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