Department of Molecular and Cellular Pharmacology, University of Miami, Miami, FL 33101, USA-
Abstract: Clathrin-mediated endocytosis is a major pathway for uptake of lipid and protein cargo at the plasma membrane- The lattices of clathrin-coated pits and vesicles are comprised of triskelions, each consisting of three oligomerized heavy chains -HC- bound by a light chain -LC-- In addition to binding HC, LC interacts with members of the Hip1-R family of endocytic proteins, including the budding yeast homologue, Sla2p- Here, using in vivo analysis in yeast, we provide novel insight into the role of this interaction- We find that overexpression of LC partially restores endocytosis to cells lacking clathrin HC- This suppression is dependent on the Sla2p binding region of LC- Using live cell imaging techniques to visualize endocytic vesicle formation, we find that the N-terminal Sla2p binding region of LC promotes the progression of arrested Sla2p patches that form in the absence of HC- We propose that LC binding to Sla2p positively regulates Sla2p for efficient endocytic vesicle formation-