Epsin but not AP-2 supports reconstitution of endocytic clathrin-coated vesicles
Formation of clathrin-coated vesicles (CCVs) in receptor-mediated endocytosis is a mechanistically well-established process, in which clathrin, the adaptor protein complex AP-2, and the large GTPase dynamin play crucial roles. In order to obtain more mechanistic insight into this process, here we es...
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| Autori principali: | , , |
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| Natura: | Article (Journal) |
| Lingua: | inglese |
| Pubblicazione: |
2020
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| In: |
FEBS letters
Year: 2020, Volume: 594, Fascicolo: 14, Pages: 2227-2239 |
| ISSN: | 1873-3468 |
| DOI: | 10.1002/1873-3468.13801 |
| Accesso online: | Verlag, kostenfrei, Volltext: https://doi.org/10.1002/1873-3468.13801 Verlag, kostenfrei, Volltext: https://onlinelibrary.wiley.com/doi/abs/10.1002/1873-3468.13801 
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| Note sull'autore: | Jan Brod, Andrea Hellwig and Felix T. Wieland |
| Riassunto: | Formation of clathrin-coated vesicles (CCVs) in receptor-mediated endocytosis is a mechanistically well-established process, in which clathrin, the adaptor protein complex AP-2, and the large GTPase dynamin play crucial roles. In order to obtain more mechanistic insight into this process, here we established a giant unilamellar vesicle (GUV)-based in vitro CCV reconstitution system with chemically defined components and the full-length recombinant proteins clathrin, AP-2, epsin-1, and dynamin-2. Our results support the predominant model in which hydrolysis of GTP by dynamin is a prerequisite to generate CCVs. Strikingly, in this system at near physiological concentrations of reagents, epsin-1 alone does not have the propensity for scission but is required for bud formation, whereas AP-2 and clathrin are not sufficient. Thus, our study reveals that epsin-1 is an important factor for the maturation of clathrin coated buds, a prerequisite for vesicle generation. |
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| Descrizione del documento: | First published: 26 April 2020 Gesehen am 12.11.2021 |
| Descrizione fisica: | Online Resource |
| ISSN: | 1873-3468 |
| DOI: | 10.1002/1873-3468.13801 |