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J Biol Chem, Vol. 273, Issue 30, 19108-19119, July 24, 1998
From the Department of Biochemistry and Biophysics and the Hormone
Research Institute, University of California,
San Francisco, California 94143-0534
The discovery of overlapping hot spots of dynamin
(Estes, P. S., Roos, J., van der Bliek, A., Kelly, R. B.,
Krishnan, K. S., and Ramaswami, M. (1996) J. Neurosci. 16, 5443-5456) and the heterotetrameric adaptor 2 complex (Gonzalez-Gaitan, M., and Jäckle, H. (1997) Cell 88, 767-776) in Drosophila nerve
terminals led to the concept of zones of active endocytosis close to
sites of active exocytosis. The proline-rich domain of Drosophila
dynamin was used to identify and purify a third component of the
endocytosis zones. Dap160 (dynamin-associated protein 160 kDa) is a
membrane-associated, dynamin-binding protein of 160 kDa that has four
putative src homology 3 domains and an Eps15 homology domain, motifs
frequently found in proteins associated with endocytosis. The binding
capacities of the four putative src homology 3 domains were examined
individually and in combination and shown to bind known proteins that
contained proline-rich domains. Each binding site, however, was
different in its preference for binding partners. We suggest that
Dap160 is a scaffolding protein that helps anchor proteins required for endocytosis at sites where they are needed in the Drosophila
nerve terminal.
Dap160, a Neural-specific Eps15 Homology and Multiple SH3
Domain-containing Protein That Interacts with Drosophila
Dynamin
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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