Dynamin and endocytosis

Curr Opin Cell Biol. 2002 Aug;14(4):463-7. doi: 10.1016/s0955-0674(02)00347-2.


The GTPase dynamin is essential for endocytosis, but its mechanism of action remains uncertain. Structures of its GTPase domain, as well as that of assembled dynamin, have led to major advances in understanding the structural basis of its mode of action. Novel data point more clearly than ever towards a role for this protein in the actin cytoskeleton, mitogen-activated protein kinase signaling and apoptosis, suggesting that dynamin might be a signaling GTPase.

Publication types

  • Review

MeSH terms

  • Animals
  • Dynamins
  • Endocytosis*
  • GTP Phosphohydrolases / chemistry
  • GTP Phosphohydrolases / metabolism*
  • Humans
  • Molecular Structure
  • Protein Conformation
  • Protein Structure, Tertiary


  • GTP Phosphohydrolases
  • Dynamins