Plasma membrane domains specialized for clathrin-mediated endocytosis in primary cells

doi:10.1074/jbc.M511370200

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Papers In Press, published online ahead of print March 13, 2006
J. Biol. Chem, 10.1074/jbc.M511370200
Submitted on October 19, 2005
Accepted on March 13, 2006

Plasma membrane domains specialized for clathrin-mediated endocytosis in primary cells

Karl D. Bellve, Deborah Leonard, Clive Standley, Lawrence M. Lifshitz, Richard A. Tuft, Akira Hayakawa, Silvia Corvera, and Kevin E. Fogarty

Program in Molecular Medicine, University of Massachusetts Medical School, Worcester, MA 01605

Corresponding Author: silvia.corvera{at}umassmed.edu

Clathrin assembly at the plasma membrane is a fundamental process required for endocytosis. In cultured cells, the majority of clathrin is localized to large patches that display little lateral mobility. The functional role of these regions is not clear, and it has been thought that they may represent artefacts of cell adhesion of cultured cells. Here we have analyzed clathrin organization in primary adipose cells isolated from mice, which are non-adherent and fully differentiated. The majority of clathrin on the plasma membrane of these cells (>60%) is found in large clathrin patches that display virtually no lateral mobility and persist for many minutes, and a smaller amount is found in small spots that appear and disappear rapidly. Direct visualization of transferrin reveals it binding onto large arrays of clathrin, and internalizing through vesicles that emerge from these domains. High resolution imaging (50 images/second) reveals fluorescence intensity fluctuations consistent with the formation and detachment of coated vesicles from within large patches. These results reveal that large clathrin assemblies are active regions of endocytosis in mammalian cells, and highlight the importance of understanding the mechanistic basis for this organization.

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