Turning on ARF: the Sec7 family of guanine-nucleotide-exchange factors

Trends Cell Biol. 2000 Feb;10(2):60-7. doi: 10.1016/s0962-8924(99)01699-2.


ARF proteins are important regulators of membrane dynamics and protein transport within the eukaryotic cell. The Sec7 domain is approximately 200 amino acids in size and stimulates guanine-nucleotide exchange on members of the ARF class of small GTPases. The members of one subclass of Sec7-domain proteins are direct targets of the secretion-inhibiting drug brefeldin A, which blocks the exchange reaction by trapping a reaction intermediate in an inactive, abortive complex. A separate subclass of Sec7-domain proteins is involved in signal transduction and possess a domain that mediates membrane binding in response to extracellular signals.

Publication types

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

MeSH terms

  • ADP-Ribosylation Factor 1 / metabolism*
  • Animals
  • Fungal Proteins / chemistry
  • Fungal Proteins / pharmacology
  • Fungal Proteins / physiology
  • Guanine Nucleotide Exchange Factors / chemistry
  • Guanine Nucleotide Exchange Factors / pharmacology
  • Guanine Nucleotide Exchange Factors / physiology
  • Humans
  • Molecular Sequence Data
  • Protein Structure, Tertiary
  • Saccharomyces cerevisiae
  • Sequence Homology, Amino Acid


  • Fungal Proteins
  • Guanine Nucleotide Exchange Factors
  • Sec7 guanine nucleotide exchange factors
  • ADP-Ribosylation Factor 1