Dynamin and its role in membrane fission.
Dynamin, a 100-kDa GTPase, is an essential component of vesicle formation in receptor-mediated endocytosis, synaptic vesicle recycling, caveolae internalization, and possibly vesicle trafficking in and out of the Golgi. In addition to the GTPase domain, dynamin also contains a pleckstrin homology domain (PH) implicated in membrane binding, a GTPase effector domain (GED) shown to be essential for self-assembly and stimulated GTPase activity, and a C-terminal proline-rich domain (PRD), which contains several SH3-binding sites. Dynamin partners bind to the PRD and may either stimulate dynamin's GTPase activity or target dynamin to the plasma membrane. Purified dynamin readily self-assembles into rings or spirals. This striking structural property supports the hypothesis that dynamin wraps around the necks of budding vesicles where it plays a key role in membrane fission. The focus of this review is on the relationship between the GTPase and self-assembly properties of dynamin and its cellular function.
Hinshaw
J E
JE
Laboratory of Cell Biochemistry and Biology, National Institutes of Health, Bethesda, Maryland 20892, USA. jennyh@helix.nih.gov
D000818:Animals; D034281:Dynamins; D020558:GTP Phosphohydrolases / Q000502:physiology*; D006801:Humans; D008561:Membrane Fusion / Q000502:physiology*; D010766:Phosphorylation; D017434:Protein Structure, Tertiary
D020558:GTP Phosphohydrolases; D034281:Dynamins