TY - JOUR TI - Epsin deficiency impairs endocytosis by stalling the actin-dependent invagination of endocytic clathrin-coated pits AU - Messa, Mirko AU - Fernández-Busnadiego, Rubén AU - Sun, Elizabeth Wen AU - Chen, Hong AU - Czapla, Heather AU - Wrasman, Kristie AU - Wu, Yumei AU - Ko, Genevieve AU - Ross, Theodora AU - Wendland, Beverly AU - De Camilli, Pietro A2 - Pfeffer, Suzanne R VL - 3 PY - 2014 DA - 2014/08/13 SP - e03311 C1 - eLife 2014;3:e03311 DO - 10.7554/eLife.03311 UR - https://doi.org/10.7554/eLife.03311 AB - 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. KW - epsin KW - actin KW - clathrin-mediated endocytosis KW - SNARE KW - Hip1R KW - cytokinesis JF - eLife SN - 2050-084X PB - eLife Sciences Publications, Ltd ER -