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

eLife

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[1] Cell Biology and Biophysics Unit, European Molecular Biology Laboratory (EMBL), Heidelberg, Germany;Department of Biochemistry, University of Geneva, Geneva, Switzerland;Department of Biochemistry, University of Geneva, Geneva, Switzerland;Cell Biology and Biophysics Unit, European Molecular Biology Laboratory (EMBL), Heidelberg, Germany;Department of Biochemistry, University of Geneva, Geneva, Switzerland;NCCR Chemical Biology, University of Geneva, Geneva, Switzerland;

关键词: endocytosis;    myosin;    actin;    S. cerevisiae;   

DOI  :  10.7554/eLife.44215

来源: publisher

【 摘 要 】

10.7554/eLife.44215.001Clathrin-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.

【 授权许可】

CC BY