Prospects & Overviews
Dynamin self-assembly and the vesicle scission mechanism
How dynamin oligomers cleave the membrane neck of clathrin-coated pits during endocytosis
Version of Record online: 18 OCT 2010
Copyright © 2010 WILEY Periodicals, Inc.
Volume 32, Issue 12, pages 1033–1039, December 2010
How to Cite
Pawlowski, N. (2010), Dynamin self-assembly and the vesicle scission mechanism. Bioessays, 32: 1033–1039. doi: 10.1002/bies.201000086
- Issue online: 18 NOV 2010
- Version of Record online: 18 OCT 2010
- guanylate binding proteins;
- immunity-related GTPases;
- Mx proteins
Recently, Gao et al. and Chappie et al. elucidated the crystal structures of the polytetrameric stalk domain of the dynamin-like virus resistance protein, MxA, and of the G-domain dimer of the large, membrane-deforming GTPase, dynamin, respectively. Combined, they provide a hypothetical oligomeric structure for the complete dynamin protein. Here, it is discussed how the oligomers are expected to form and how they participate in dynamin mediated vesicle fission during the process of endocytosis. The proposed oligomeric structure is compared with the novel mechanochemical model of dynamin function recently proposed by Bashkirov et al. and Pucadyil and Schmid. In conclusion, the new model of the dynamin oligomer has the potential to explain how short self-limiting fissogenic dynamin assemblies are formed and how concerted GTP hydrolysis is achieved. The oligomerisation of two other dynamin superfamily proteins, the guanylate binding proteins (GBPs) and the immunity-related GTPases (IRGs), is addressed briefly.