Epsin deficiency impairs endocytosis by stalling the actin-dependent invagination of endocytic clathrin-coated pits
2014
Mirko Messa | Rubén Fernández-Busnadiego | Elizabeth Wen Sun | Hong Chen | Heather Czapla | Kristie Wrasman | Yumei Wu | Genevieve Ko | Theodora Ross | Beverly Wendland | Pietro De Camilli
Epsin is an evolutionarily conserved endocytic clathrin adaptor whose most critical function(s) in clathrin coat dynamics remain(s) elusive. To elucidate such function(s), we generated embryonic fibroblasts from conditional epsin triple KO mice. Triple KO cells displayed a dramatic cell division defect. Additionally, a robust impairment in clathrin-mediated endocytosis was observed, with an accumulation of early and U-shaped pits. This defect correlated with a perturbation of the coupling between the clathrin coat and the actin cytoskeleton, which we confirmed in a cell-free assay of endocytosis. Our results indicate that a key evolutionary conserved function of epsin, in addition to other roles that include, as we show here, a low affinity interaction with SNAREs, is to help generate the force that leads to invagination and then fission of clathrin-coated pits.
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