Membrane recruitment of effector proteins by Arf and Rab GTPases

Curr Opin Struct Biol. 2005 Dec;15(6):681-9. doi: 10.1016/ Epub 2005 Nov 9.


In their GTP-bound form, Arf and Rab family GTPases associate with distinct organelle membranes, to which they recruit specific sets of effector proteins that regulate vesicular transport. The Arf GTPases are involved in the formation of coated carrier vesicles by recruiting coat proteins. On the other hand, the Rab GTPases are involved in the tethering, docking and fusion of transport vesicles with target organelles, acting in concert with the tethering and fusion machineries. Recent structural studies of the Arf1-GGA and Rab5-Rabaptin-5 complexes, as well as other effector structures in complex with the Arf and Rab GTPases, have shed light on the mechanisms underlying the GTP-dependent membrane recruitment of these effector proteins.

Publication types

  • Review

MeSH terms

  • ADP-Ribosylation Factor 1 / metabolism
  • ADP-Ribosylation Factors / metabolism*
  • Adaptor Proteins, Vesicular Transport / metabolism
  • Animals
  • Humans
  • Intracellular Membranes / metabolism*
  • Models, Molecular
  • Protein Binding
  • Protein Conformation
  • Protein Transport
  • Vesicular Transport Proteins / metabolism
  • rab GTP-Binding Proteins / metabolism*
  • rab5 GTP-Binding Proteins / metabolism


  • Adaptor Proteins, Vesicular Transport
  • GGA adaptor proteins
  • RABEP1 protein, human
  • Vesicular Transport Proteins
  • ADP-Ribosylation Factor 1
  • ADP-Ribosylation Factors
  • rab GTP-Binding Proteins
  • rab5 GTP-Binding Proteins