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(Received for publication, December 23, 1996, and in revised form, March 13, 1997)
From the Amphiphysin is an SH3 domain-containing neuronal
protein that is highly concentrated in nerve terminals where it
interacts via its SH3 domain with dynamin I, a GTPase implicated in
synaptic vesicle endocytosis. We show here that the SH3 domain of
amphiphysin, but not a mutant SH3 domain, bound with high affinity to a
single site in the long proline-rich region of human dynamin I, that this site was distinct from the binding sites for other SH3 domains, and that the mutation of two adjacent amino acids in dynamin I was
sufficient to abolish binding. The dynamin I sequence critically required for amphiphysin binding (PSRPNR) fits in the novel SH3 binding
consensus identified for the SH3 domain of amphiphysin via a
combinatorial peptide library approach:
PXRPXR(H)R(H). Our data demonstrate that the
long proline-rich stretch present in dynamin I contained multiple SH3
domain binding sites that recognize interacting proteins with high
specificity.
Volume 272, Number 20,
Issue of May 16, 1997
pp. 13419-13425
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
,
,
,
Department of Cell Biology and Howard Hughes
Medical Institute, Yale University School of Medicine, Boyer Center
for Molecular Medicine, New Haven, Connecticut 06510 and the
¶ Department of Cell Biology, Harvard Medical School,
Boston, Massachusetts 02115
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E. B. Ives, J. Nichols, S. R. Wente, and J. D. York Biochemical and Functional Characterization of Inositol 1,3,4,5,6-Pentakisphosphate 2-Kinases J. Biol. Chem., November 17, 2000; 275(47): 36575 - 36583. [Abstract] [Full Text] [PDF]
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