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SH3 domain‐dependent interactions of endophilin with amphiphysin
Author(s) -
Kristina D. Micheva,
Antoine R. Ramjaun,
Brian K. Kay,
Peter S. McPherson
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(97)01016-8
Subject(s) - amphiphysin , endocytosis , sh3 domain , synaptic vesicle , chemistry , phosphoprotein , signal transducing adaptor protein , microbiology and biotechnology , biophysics , biochemistry , phosphorylation , dynamin , biology , vesicle , receptor , proto oncogene tyrosine protein kinase src , membrane
Amphiphysin I and II are nerve terminal‐enriched proteins thought to function in synaptic vesicle endocytosis. In addition to a C‐terminal SH3 domain, the proteins contain a highly conserved putative SH3 binding site and numerous consensus phosphorylation sites. We now demonstrate that amphiphysin I but not amphiphysin II is a phosphoprotein which undergoes dephosphorylation during nerve terminal depolarization. Further, both amphiphysin I and II interact with the SH3 domain of endophilin, a synaptically enriched protein implicated in synaptic vesicle endocytosis. The interaction is direct and mediated through a 43 amino acid region of amphiphysin containing the putative SH3 binding site. These data further support a role for amphiphysin I, II and endophilin in synaptic vesicle endocytosis.