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Vol. 11, Issue 6, 2151-2159, June 2000
*Department of Biology, Vassar College, Poughkeepsie, New York
12604; and Clathrin-coated vesicles bud from selected cellular membranes to
traffic-specific intracellular proteins. To study the dynamic properties of clathrin-coated membranes, we expressed clathrin heavy
chain tagged with green fluorescent protein (GFP) in
Dictyostelium cells. GFP-clathrin was functional and
retained the native properties of clathrin: the chimeric protein formed
classic clathrin lattices on cellular membranes and also rescued
phenotypic defects of clathrin null cells. GFP-clathrin distributed
into punctate loci found throughout the cytoplasm, on the plasma
membrane, and concentrated to a perinuclear location. These
clathrin-coated structures were remarkably motile and capable of rapid
and bidirectional transport across the cell. We identified two local
domains of the plasma membrane as sites for clathrin recruitment in
motile cells. First, as cells translocated or changed shape and
retracted their tails, clathrin was transiently concentrated on the
membrane at the back of the cell tail. Second, as cells capped their
cell surface receptors, clathrin was recruited locally to the membrane
under the tight cap of cross-linked receptors. This suggests that local
sites for clathrin polymerization on specific domains of the plasma membrane undergo rapid and dynamic regulation in motile cells.
Section of Molecular Cell and Developmental
Biology, Institute of Cellular and Molecular Biology, The University of
Texas at Austin, Austin, Texas 78712
Online version of this article contains video material
for Figures 4-6. Online version available at
www.molbiolcell.org.
Corresponding author. E-mail
address: t.ohalloran{at}mail.utexas.edu.
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