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Originally published as MBC in Press, 10.1091/mbc.E04-08-0739 on February 2, 2005

Vol. 16, Issue 4, 1769-1776, April 2005

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Highly Cooperative Control of Endocytosis by Clathrin{boxd}

Howard S. Moskowitz, Charles T. Yokoyama, and Timothy A. Ryan

Department of Biochemistry, Weill Medical College of Cornell University, New York, NY 10021

Submitted August 25, 2004; Revised December 28, 2004; Accepted January 17, 2005
Monitoring Editor: Keith Mostov

Clathrin assembles into a dynamic two-dimensional lattice on the plasma membrane where it plays a critical role in endocytosis. To probe the regulation of this process, we used siRNA against clathrin, in combination with single cell assays for transferrin uptake as well as total internal reflection microscopy, to examine how endocytic rates and membrane dynamics depend upon cellular clathrin concentration ([Clathrin]). We find that endocytosis is tightly controlled by [Clathrin] over a very narrow dynamic range such that small changes in [Clathrin] can lead to large changes in endocytic rates, indicative of a highly cooperative process (apparent Hill coefficient, n > 6). The number of clathrin assemblies at the cell surface was invariant over a wide range of [Clathrin]; however, both the amount of clathrin in each assembly and the subsequent membrane dynamics were steeply dependent on [Clathrin]. Thus clathrin controls the structural dynamics of membrane internalization via a strongly cooperative process. We used this analysis to show that one important regulator of endocytosis, the actin cytoskeleton, acts noncompetitively as a modulator of clathrin function.

This article was published online ahead of print in MBC in Press (http://www.molbiolcell.org/cgi/doi/10.1091/mbc.E04–08–0739) on February 2, 2005.

{boxd} The online version of this article contains supplemental material at MBC Online (http://www.molbiolcell.org).

Address correspondence to: Timothy A. Ryan (taryan{at}med.cornell.edu).




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