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J. Biol. Chem., Vol. 281, Issue 23, 16139-16146, June 9, 2006

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Plasma Membrane Domains Specialized for Clathrin-mediated Endocytosis in Primary Cells^*

Karl D. Bellve¹, Deborah Leonard¹, Clive Standley, Lawrence M. Lifshitz, Richard A. Tuft, Akira Hayakawa^¶, Silvia Corvera^¶2, and Kevin E. Fogarty

From the Departments of Physiology and ^¶Molecular Medicine and the Interdisciplinary Graduate Program, University of Massachusetts Medical School, Worcester, Massachusetts 01605

Clathrin assembly at the plasma membrane is a fundamental process required for endocytosis. In cultured cells, most of the 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 artifacts of cell adhesion of cultured cells. Here we have analyzed clathrin organization in primary adipose cells isolated from mice, which are nonadherent and fully differentiated. The majority of clathrin on the plasma membrane of these cells (>60%) was found in large clathrin patches that displayed virtually no lateral mobility and persisted for many minutes, and a smaller amount was found in small spots that appeared and disappeared rapidly. Direct visualization of transferrin revealed that it bound onto large arrays of clathrin, internalizing through vesicles that emerge from these domains. High resolution imaging (50 images/s) revealed 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.

Received for publication, October 19, 2005 , and in revised form, February 2, 2006.

^* This work was supported by National Institutes of Health Grant PO1 DK60564 (to S. C. and K. E. F.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ These authors contributed equally to this work.

² To whom correspondence should be addressed: Program in Molecular Medicine, University of Massachusetts Medical School, 373 Plantation St., Worcester, MA 01605. E-mail: silvia.corvera{at}umassmed.edu.

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