Identification and Characterization of a Nerve Terminal-enriched Amphiphysin Isoform
Open accessAbstract
Amphiphysin is a nerve terminal-enriched protein thought to function in synaptic vesicle endocytosis, in part through Src homology 3 (SH3) domain-mediated interactions with dynamin and synaptojanin. Here, we report the characterization of a novel amphiphysin isoform (termed amphiphysin II) that was identified through a homology search of the data base of expressed sequence tags. Antibodies specific to amphiphysin II recognize a 90-kDa protein on Western blot that is brain-specific and highly enriched in nerve terminals. Like amphiphysin (now referred to as amphiphysin I), amphiphysin II binds to dynamin and synaptojanin through its SH3 domain. Further, both proteins bind directly to clathrin in an SH3 domain-independent manner. Taken together, these data suggest that amphiphysin II may participate with amphiphysin I in the regulation of synaptic vesicle endocytosis.
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BIN1 undergoes complex alternative splicing to generate multiple isoforms with diverse functions in multiple cellular processes including endocytosis and membrane remodeling.
“BIN1 undergoes complex alternative splicing to generate multiple isoforms with diverse functions in multiple cellular processes including endocytosis and membrane remodeling.”
From Predominant expression of Alzheimer’s disease-associated BIN1 in mature oligodendrocytes and localization to white matter tracts (2016) · cites this paper as [5]
The Results and Discussion (page not available in our copy) identify BIN1, SH3P9, and amphiphysin II as likely products of alternative splicing, with distinct properties. The Discussion suggests a role for amphiphysin II in synaptic vesicle endocytosis, but the paper does not establish membrane remodeling as a function of these isoforms or support the broader claim that they have diverse functions across multiple cellular processes. (LLM, conf=0.86)
Experimental — accuracy not yet measuredA 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 [5]
The Results (page unavailable) describe an SH3-domain region conserved among amphiphysin II, BIN1, and SH3P9; they also show that amphiphysin II’s SH3 domain binds dynamin and synaptojanin. The paper does not establish binding by every BIN1 isoform and does not report an interaction with endophilin. (LLM, conf=0.88)
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Research works printed but not linked: 4
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“Whereas BIN1 expression in brain has been previously reported, the cellular profile of BIN1 expression in human has not been characterized in detail [4, 5, 12, 26, 30].”
Functional coordination of alternative splicing in the mammalian central nervous system
Fagnani, M., Barash, Y., Ip, J. Y., Misquitta, C., Pan, Q., Saltzman, A. L., Shai, O., Lee, L., Rozenhek, A., Mohammad, N., et al. (2007) · Genome Biology · doi:10.1186/gb-2007-8-6-r108 · Cited by 120 · see citing works
SH3 domain‐dependent interactions of endophilin with amphiphysin
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Self-citationSartori, M., Mendes, T., Desai, S., Lasorsa, A., Herledan, A., Malmanche, N., Mäkinen, P., Marttinen, M., Malki, I., Chapuis, J., et al. (2019) · Acta Neuropathologica · doi:10.1007/s00401-019-02017-9 · Cited by 72 · see citing works
- Authors
- Ramjaun, A. R., Micheva, K. D., Bouchelet, I., & McPherson, P. S.
- Affiliations
- Montreal Neurological Institute and Hospital (CA)
- Corresponding author
- McPherson, Peter S.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1997-06
- Volume
- 272
- Issue
- 26
- Pages
- 16700-16706
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1995025647
- Cited by
- 192
- References
- 0
- Citations by year
- 2026: 2 · 2025: 7 · 2024: 1 · 2023: 2 · 2022: 14 · 2021: 3 · 2020: 4 · 2019: 10 · 2018: 1 · 2017: 3 · 2016: 4 · 2015: 3 · 2014: 3 · 2013: 2 · 2012: 5
- FWCI
- 5.68
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- Yale University
- Medical Research Council Canada
- Medical Research Council
- 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 › Cell Biology › Caveolin-1 and cellular processes
- Keywords
- presynaptic terminals, synaptic vesicle endocytosis, SH3 domain, dynamin, synaptojanin, clathrin, brain-specific proteins, expressed sequence tags
- MeSH terms
- Amino Acid Sequence, Animals, Base Sequence, Brain Chemistry, Clathrin, Endocytosis, Molecular Sequence Data, Nerve Tissue Proteins, Phosphoric Monoester Hydrolases, Synaptic Vesicles, src Homology Domains, GTP Phosphohydrolases, Dynamins, Rats
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