SH3 domain‐dependent interactions of endophilin with amphiphysin
Open accessAbstract
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.
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A C-terminal SH3 domain found in all BIN1 isoforms mediates interaction with proteins involved in endocytosis such as dynamin, synaptojanin, and endophilin.
“A C-terminal SH3 domain, also found in all isoforms, mediates BIN1 interaction with proteins involved in endocytosis, such as dynamin, synaptojanin, and endophilin [1, 4–6, 14].”
From Predominant expression of Alzheimer’s disease-associated BIN1 in mature oligodendrocytes and localization to white matter tracts (2016) · cites this paper as [14]
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- Authors
- Micheva, K. D., Ramjaun, A. R., Kay, B. K., & McPherson, P. S.
- Affiliations
- Montreal Neurological Institute and Hospital (CA)
- University of North Carolina at Chapel Hill (US)
- Venue
- FEBS Letters
- Publisher
- Wiley
- Published
- 1997-09-08
- Volume
- 414
- Issue
- 2
- Pages
- 308-312
- ISSN
- 0014-5793 (ISSN-L)
- 1873-3468
- OpenAlex
- W2020167482
- Cited by
- 91
- References
- 21
- Citations by year
- 2026: 2 · 2025: 3 · 2024: 4 · 2023: 8 · 2022: 2 · 2020: 1 · 2017: 3 · 2016: 4 · 2015: 2 · 2014: 5 · 2012: 2
- FWCI
- 1.73
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- FEBS Letters (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Keywords
- endophilin, SH3 domain, protein-protein interaction, synaptic vesicle endocytosis, dephosphorylation, phosphorylation sites, synapses
- MeSH terms
- Amino Acid Sequence, Animals, Antibodies, Base Sequence, Binding Sites, Brain, Carrier Proteins, Endocytosis, Glutathione Transferase, Molecular Sequence Data, Nerve Tissue Proteins, Peptide Fragments, Phosphoproteins, Phosphorylation, Recombinant Fusion Proteins, Synaptic Vesicles, Synaptosomes, Polymerase Chain Reaction, DNA Primers, src Homology Domains, Adaptor Proteins, Signal Transducing, Rats
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