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Vol. 17, Issue 10, 4343-4352, October 2006
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*Department of Molecular and Cellular Pharmacology, University of Miami, Miami, FL 33101; and Instituto de Biología Molecular de Barcelona (IBMB), Consejo Superior de Investigaciones Científicas, 08034 Barcelona, Spain
Submitted July 17, 2006;
Accepted July 19, 2006
Monitoring Editor: Sandra Schmid
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.
The online version of this contains supplemental material at MBC Online (http://www.molbiolcell.org). This article was published online ahead of print in MBC in Press (http://www.molbiolcell.org/cgi/doi/10.1091/mbc.E06-07-0606) on July 26, 2006.
Address correspondence to: Sandra K. Lemmon (slemmon{at}miami.edu)
Abbreviations used: HC, heavy chain; LC, light chain; CCV, clathrin-coated vesicle; TGN, trans-Golgi network; WT, wild type; GFP, green fluorescence protein; RFP, red fluorescence protein; GST, glutathione-S-transferase; USH, upstream alpha helix; THATCH, talin-Hip1/R/Sla2p actin-tethering C-terminal homology.
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