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    FEBS Lett. 1997 Sep 8;414(2):308-12.

    SH3 domain-dependent interactions of endophilin with amphiphysin.

    Micheva KD, Ramjaun AR, Kay BK, McPherson PS.

    Department of Neurology and Neurosurgery, Montreal Neurological Institute, McGill University, Que., Canada.

    Erratum in:

    • FEBS Lett 1997 Dec 8;419(1):150.

    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.

    PMID: 9315708 [PubMed - indexed for MEDLINE]

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