Arf-like GTPases: not so Arf-like after all

Trends Cell Biol. 2004 Dec;14(12):687-94. doi: 10.1016/j.tcb.2004.10.004.


ADP-ribosylation factor (Arf) GTP-binding proteins are among the best-characterized members of the Ras superfamily of GTPases, with well-established functions in membrane-trafficking pathways. A recent watershed of genomic and structural information has identified a family of conserved related proteins: the Arf-like (Arl) GTPases. The best-characterized Arl protein, Arl2, regulates the folding of beta tubulin, and recent data suggest that Arl1 and Arf-related protein 1 (ARFRP1) are localized to the trans-Golgi network (TGN), where they function, in part, to regulate the tethering of endosome-derived transport vesicles. Other Arl proteins are localized to the cytosol, nucleus, cytoskeleton and mitochondria, which indicates that Arl proteins have diverse roles that are distinct from the known functions of traditional Arf GTPases.

Publication types

  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • ADP-Ribosylation Factors / metabolism
  • ADP-Ribosylation Factors / physiology*
  • Animals
  • GTP Phosphohydrolases / metabolism
  • GTP Phosphohydrolases / physiology*
  • Humans
  • Membrane Proteins / metabolism
  • Membrane Proteins / physiology*
  • Protein Structure, Secondary
  • Saccharomyces cerevisiae / metabolism
  • Saccharomyces cerevisiae Proteins / physiology


  • Membrane Proteins
  • Saccharomyces cerevisiae Proteins
  • ADP-ribosylation factor related proteins
  • GTP Phosphohydrolases
  • ADP-Ribosylation Factors