SH3 domain-dependent interactions of endophilin with amphiphysin.
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.
Mesh Terms:
Adaptor Proteins, Signal Transducing, Amino Acid Sequence, Animals, Antibodies, Base Sequence, Binding Sites, Brain, Carrier Proteins, DNA Primers, Endocytosis, Glutathione Transferase, Molecular Sequence Data, Nerve Tissue Proteins, Peptide Fragments, Phosphoproteins, Phosphorylation, Polymerase Chain Reaction, Rats, Recombinant Fusion Proteins, Synaptic Vesicles, Synaptosomes, src Homology Domains
Adaptor Proteins, Signal Transducing, Amino Acid Sequence, Animals, Antibodies, Base Sequence, Binding Sites, Brain, Carrier Proteins, DNA Primers, Endocytosis, Glutathione Transferase, Molecular Sequence Data, Nerve Tissue Proteins, Peptide Fragments, Phosphoproteins, Phosphorylation, Polymerase Chain Reaction, Rats, Recombinant Fusion Proteins, Synaptic Vesicles, Synaptosomes, src Homology Domains
FEBS Lett.
Date: Sep. 08, 1997
PubMed ID: 9315708
View in: Pubmed Google Scholar
Download Curated Data For This Publication
10263
Switch View:
- Interactions 1