Cooperative Recruitment of Dynamin and BIN/Amphiphysin/Rvs (BAR) Domain-containing Proteins Leads to GTP-dependent Membrane Scission*
Open accessAbstract
Dynamin mediates various membrane fission events, including the scission of clathrin-coated vesicles. Here, we provide direct evidence for cooperative membrane recruitment of dynamin with the BIN/amphiphysin/Rvs (BAR) proteins, endophilin and amphiphysin. Surprisingly, endophilin and amphiphysin recruitment to membranes was also dependent on binding to dynamin due to auto-inhibition of BAR-membrane interactions. Consistent with reciprocal recruitment in vitro, dynamin recruitment to the plasma membrane in cells was strongly reduced by concomitant depletion of endophilin and amphiphysin, and conversely, depletion of dynamin dramatically reduced the recruitment of endophilin. In addition, amphiphysin depletion was observed to severely inhibit clathrin-mediated endocytosis. Furthermore, GTP-dependent membrane scission by dynamin was dramatically elevated by BAR domain proteins. Thus, BAR domain proteins and dynamin act in synergy in membrane recruitment and GTP-dependent vesicle scission.
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The SH3 domain regulates the conformation of the BAR domain and its interaction with other molecules.
“In addition, the SH3 domain regulates the conformation of the BAR domain and its interaction with other molecules (34,35).”
From BIN1 regulates BACE1 intracellular trafficking and amyloid-β production (2016) · cites this paper as [35]
The Results and Discussion (page unavailable) show that SH3 domains inhibit membrane binding by endophilin and amphiphysin, and that binding dynamin’s proline-rich domain to SH3 reverses this inhibition. The paper suggests an SH3–BAR interaction but does not establish that SH3 regulates the BAR domain’s conformation. (LLM, conf=0.86)
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- Authors
- Meinecke, M., Boucrot, E., Camdere, G., Hon, W.-C., Mittal, R., & McMahon, H. T.
- Affiliations
- MRC Laboratory of Molecular Biology (GB)
- Corresponding author
- Meinecke, Michael
- McMahon, Harvey T.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2013-03
- Volume
- 288
- Issue
- 9
- Pages
- 6651-6661
- ISSN
- 0021-9258 (ISSN-L)
- PMC
- PMC3585104
- OpenAlex
- W2088954489
- Cited by
- 155
- References
- 47
- Citations by year
- 2026: 6 · 2025: 5 · 2024: 7 · 2023: 5 · 2022: 11 · 2021: 18 · 2020: 12 · 2019: 10 · 2018: 16 · 2017: 11 · 2016: 11 · 2015: 14 · 2014: 19 · 2013: 9
- FWCI
- 10.25
- Type
- journal article
- Language
- en
- Update notices
- erratum (2026-10-01)
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by-nc)
- PubMed Central (publishedVersion, cc-by-nc)
- PubMed (publishedVersion)
- UCL Discovery (University College London) (submittedVersion)
- GRO (submittedVersion, cc-by)
- Funders
- Deutsche Forschungsgemeinschaft (SFB803)
- Medical Research Council (U105178805)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Lipid Membrane Structure and Behavior
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Caveolin-1 and cellular processes
- Keywords
- dynamin, BAR domain proteins, endophilin, amphiphysin, membrane fission, membrane recruitment, clathrin-mediated endocytosis, clathrin-coated vesicles, protein-protein interaction
- MeSH terms
- Cell Line, Cell Membrane, Guanosine Triphosphate, Humans, Nerve Tissue Proteins, Secretory Vesicles, Dynamins
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