Dynamin and its role in membrane fission

Annu Rev Cell Dev Biol. 2000;16:483-519. doi: 10.1146/annurev.cellbio.16.1.483.

Abstract

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.

Publication types

  • Review

MeSH terms

  • Animals
  • Dynamins
  • GTP Phosphohydrolases / physiology*
  • Humans
  • Membrane Fusion / physiology*
  • Phosphorylation
  • Protein Structure, Tertiary

Substances

  • GTP Phosphohydrolases
  • Dynamins