The amphiphysin family of proteins and their role in endocytosis at the synapse
Abstract
Clathrin-mediated endocytosis at the plasma membrane is a major pathway of synaptic vesicle recycling in neurones, but little is known about the molecular machinery that orchestrates the process. The amphiphysin protein has recently emerged into the limelight since its discovery in 1992 as a synaptic vesicle-associated protein. It was subsequently found to interact in vitro with the GTPase dynamin through its SH3 domain. However, only in the past year has its role in endocytosis been confirmed, with the demonstration that the introduction of dominant-negative-acting SH3 domains into living cells causes a potent blockade of clathrin-mediated endocytosis. This, together with the discovery by several groups of a second nerve terminal-enriched amphiphysin isoform, and the finding that the two proteins heterodimerize, further suggests that the amphiphysins are closely connected with dynamin-mediated vesicle budding. This review summarizes current views in the field, and draws on data that suggest intriguing alternative roles--including possible involvement in the cytoskeleton and in tumour suppression--for certain members of the amphiphysin family.
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The CLAP domain, encoded by alternatively spliced exons present only in neuronal BIN1 isoforms, is important for BIN1's function in clathrin-mediated endocytosis and synaptic vesicle recycling.
“The CLathrin-Associated Protein binding region (CLAP domain), encoded by alternatively spliced exons present only in the neuronal BIN1 isoforms, is important for BIN1’s function in clathrin-mediated endocytosis and synaptic vesicle recycling [1, 9].”
From Predominant expression of Alzheimer’s disease-associated BIN1 in mature oligodendrocytes and localization to white matter tracts (2016) · cites this paper as [9]
The section “Potential interactions with other elements of the endocytotic apparatus” (p. 3) reports that Amph2/BIN1 binds clathrin through central sequences and that several non-neuronal splice forms do not bind clathrin. The review connects amphiphysins with endocytosis at nerve terminals, but it does not identify a CLAP domain, establish that its exons occur only in neuronal isoforms, or demonstrate that this domain is important for BIN1-mediated vesicle recycling. (LLM, conf=0.86)
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References 59 · Cited by 247
Research works printed but not linked: 4
- 15 Urrutia, R. et al. (1997) Proc. Natl. Acad. Sci. U. S. A. 94, 377-384
- 20 David, C. et al. (1996) Proc. Natl. Acad. Sci. U. S. A. 93, 331-335
- 33 Owen, D.J. et al. EMBO J. (in press)
- 49 Kadlec, L. and Pendergast, A.M. (1997) Proc. Natl. Acad. Sci. U. S. A. 94, 12390-12395
- Authors
- Wigge, P., & McMahon, H. T.
- Affiliations
- MRC Laboratory of Molecular Biology (GB)
- ORCID
- McMahon, Harvey T.
- Venue
- Trends in Neurosciences
- Publisher
- Elsevier BV
- Published
- 1998-08
- Volume
- 21
- Issue
- 8
- Pages
- 339-344
- ISSN
- 0166-2236 (ISSN-L)
- OpenAlex
- W2136203552
- Cited by
- 247
- References
- 59
- Citations by year
- 2026: 3 · 2025: 1 · 2024: 2 · 2023: 6 · 2022: 2 · 2021: 3 · 2020: 3 · 2019: 6 · 2018: 2 · 2017: 1 · 2016: 8 · 2015: 8 · 2014: 9 · 2013: 6 · 2012: 5
- FWCI
- 1.89
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Trends in Neurosciences (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 › Cell Biology › Caveolin-1 and cellular processes
- Keywords
- amphiphysin, clathrin-mediated endocytosis, synaptic vesicle recycling, synapses, dynamin, SH3 domain, heterodimerization, vesicle budding, cytoskeleton, tumor suppression, neurons
- MeSH terms
- Animals, Endocytosis, Humans, Nerve Tissue Proteins, Phosphorylation, Synapses
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