The DOI matches its Crossref record; 35 of the 35 references it cites were found in a registry or an index.
Amphiphysin Heterodimers: Potential Role in Clathrin-mediated Endocytosis
Open accessAbstract
Amphiphysin (Amph) is a src homology 3 domain-containing protein that has been implicated in synaptic vesicle endocytosis as a result of its interaction with dynamin. In a screen for novel members of the amphiphysin family, we identified Amph2, an isoform 49% identical to the previously characterized Amph1 protein. The subcellular distribution of this isoform parallels Amph1, both being enriched in nerve terminals. Like Amph1, a role in endocytosis at the nerve terminal is supported by the rapid dephosphorylation of Amph2 on depolarization. Importantly, the two isoforms can be coimmunoprecipitated from the brain as an equimolar complex, suggesting that the two isoforms act in concert. As determined by cross-linking of brain extracts, the Amph1–Amph2 complex is a 220- to 250-kDa heterodimer. COS cells transfected with either Amph1 or Amph2 show greatly reduced transferrin uptake, but coexpression of the two proteins rescues this defect, supporting a role for the heterodimer in clathrin-mediated endocytosis. Although the src homology 3 domains of both isoforms interact with dynamin, the heterodimer can associate with multiple dynamin molecules in vitro and activates dynamin’s GTPase activity. We propose that it is an amphiphysin heterodimer that drives the recruitment of dynamin to clathrin-coated pits in endocytosing nerve terminals.
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Cites
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Cited by
Doherty, G. J., & McMahon, H. T. (2009) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.78.081307.110540 · Cited by 3,075
Self-citationMolecular mechanism and physiological functions of clathrin-mediated endocytosis
McMahon, H. T., & Boucrot, E. (2011) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3151 · Cited by 2,223
Self-citationEpidemiology of Alzheimer disease
Reitz, C., Brayne, C., & Mayeux, R. (2011) · Nature Reviews Neurology · doi:10.1038/nrneurol.2011.2 · Cited by 1,675
BAR Domains as Sensors of Membrane Curvature: The Amphiphysin BAR Structure
Peter, B. J., Kent, H. M., Mills, I. G., Vallis, Y., Butler, P. J. G., Evans, P. R., & McMahon, H. T. (2004) · Science · doi:10.1126/science.1092586 · Cited by 1,636
Self-citationGenome-wide Analysis of Genetic Loci Associated With Alzheimer Disease
Seshadri, S. (2010) · JAMA · doi:10.1001/jama.2010.574 · Cited by 1,219
Metadata
- Authors
- Wigge, P., Köhler, K., Vallis, Y., Doyle, C. A., Owen, D., Hunt, S. P., & McMahon, H. T.
- Venue
- Molecular Biology of the Cell
- Published
- 1997-10
- Volume
- 8
- Issue
- 10
- Pages
- 2003-2015
- ISSN
- 1059-1524 (ISSN-L)
- 1939-4586
- OpenAlex
- W2163777695
- Cited by
- 265
- References
- 35
- FWCI
- 6.04
- Type
- journal article
- Language
- en
- Open access
- green
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- Wigge, P., Köhler, K., Vallis, Y., Doyle, C. A., Owen, D., Hunt, S. P., & McMahon, H. T. (1997). Amphiphysin Heterodimers: Potential Role in Clathrin-mediated Endocytosis. Molecular Biology of the Cell. https://doi.org/10.1091/mbc.8.10.2003
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