The dynamin superfamily

Curr Biol. 2018 Apr 23;28(8):R411-R416. doi: 10.1016/j.cub.2017.12.013.


The dynamin superfamily comprises a growing assortment of multi-domain GTPases, found from bacteria to man, that are distinguished from typical GTPases of the Ras, Rab and G-protein families by their modular structure (Figure 1), relatively large size (>70 kDa), and low affinity for guanine nucleotides. In addition, they display a conserved propensity to self-assemble into polymeric arrays, the dynamics of which are regulated by an autonomous, assembly-stimulated GTPase activity.

Publication types

  • Review

MeSH terms

  • Amino Acid Motifs
  • Conserved Sequence
  • Dynamins / metabolism*
  • Dynamins / physiology*
  • Dynamins / ultrastructure*
  • GTP Phosphohydrolases / metabolism
  • GTP Phosphohydrolases / physiology
  • Guanosine Triphosphate / metabolism


  • Guanosine Triphosphate
  • GTP Phosphohydrolases
  • Dynamins