ARF family G proteins and their regulators: roles in membrane transport, development and disease

Nat Rev Mol Cell Biol. 2011 Jun;12(6):362-75. doi: 10.1038/nrm3117. Epub 2011 May 18.


Members of the ADP-ribosylation factor (ARF) family of guanine-nucleotide-binding (G) proteins, including the ARF-like (ARL) proteins and SAR1, regulate membrane traffic and organelle structure by recruiting cargo-sorting coat proteins, modulating membrane lipid composition, and interacting with regulators of other G proteins. New roles of ARF and ARL proteins are emerging, including novel functions at the Golgi complex and in cilia formation. Their function is under tight spatial control, which is mediated by guanine nucleotide exchange factors (GEFs) and GTPase-activating proteins (GAPs) that catalyse GTP exchange and hydrolysis, respectively. Important advances are being gained in our understanding of the functional networks that are formed not only by the GEFs and GAPs themselves but also by the inactive forms of the ARF proteins.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • ADP-Ribosylation Factors / metabolism*
  • Animals
  • Biological Transport, Active
  • Cell Membrane / metabolism*
  • GTPase-Activating Proteins / metabolism
  • Golgi Apparatus / metabolism
  • Guanine Nucleotide Exchange Factors / metabolism
  • Humans
  • Membrane Lipids / metabolism
  • Membrane Proteins / metabolism
  • Mice
  • Monomeric GTP-Binding Proteins / metabolism
  • Neurodegenerative Diseases / metabolism


  • GTPase-Activating Proteins
  • Guanine Nucleotide Exchange Factors
  • Membrane Lipids
  • Membrane Proteins
  • ADP-ribosylation factor related proteins
  • SAR1A protein, human
  • ADP-Ribosylation Factors
  • Monomeric GTP-Binding Proteins