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(Received for publication, August 30, 1996, and in revised form, September 19, 1996)
From the Eps15, a phosphorylation substrate of the
epidermal growth factor (EGF) receptor kinase, has been shown to bind
to the
Volume 271, Number 46,
Issue of November 15, 1996
pp. 28727-28730
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
COMMUNICATION:
,
,
,
and**
Department of Pharmacology, University
of Colorado Health Sciences Center, Denver, Colorado 80262, the
Department of Cell Biology, Harvard Medical School,
Boston, Massachusetts 02115, and the ** Center for Blood
Research, Boston, Massachusetts 02115
-subunit of the clathrin-associated protein complex AP-2.
Here we report that in cells, virtually all Eps15 interacts with the
cytosol and membrane-bound forms of AP-2. This association is not
affected by the treatment of cells with EGF. Immunofluorescence
microscopy reveals nearly absolute co-localization of Eps15 with AP-2
and clathrin, and analysis by immunoelectron microscopy shows that the
localization of membrane-associated Eps15 is restricted to the profiles
corresponding to endocytic coated pits and vesicles. Unexpectedly,
Eps15 was found at the edge of forming coated pits and at the rim of
budding coated vesicles. This asymmetric distribution is in sharp
contrast to the localization of AP-2 that shows an even distribution
along the same types of clathrin-coated structures. These findings
suggest several possible regulatory roles of Eps15 during the formation
of coated pits.
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T Sorkina, A Bild, F Tebar, and A Sorkin Clathrin, adaptors and eps15 in endosomes containing activated epidermal growth factor receptors J. Cell Sci., January 2, 1999; 112(3): 317 - 327. [Abstract] [PDF]
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