ADP-ribosylation factors: a family of ∼20-kDa guanine nucleotide-binding proteins that activate cholera toxin

Catherine F. Welsh, Joel Moss, Martha Vaughan

Research output: Contribution to journalArticle

43 Scopus citations

Abstract

ADP-ribosylation factors (ARFs) comprise a family of ∼20 kDa guanine nucleotide-binding proteins that were discovered as one of several cofactors required in cholera toxin-catalyzed ADP-ribosylation of G, the guanine nucleotide-binding protein responsible for stimulation of adenylyl cyclase, and was subsequently found to enhance all cholera toxin-catalyzed reactions and to directly interact with, and activate the toxin. ARF is dependent on GTP or its analogues for activity, binds GTP with high affinity in the presence of dimyristoylphosphatidylcholine/cholate and contains consensus sequences for GTP-binding and hydrolysis. Six mammalian family members have been identified which have been classified into three groups (Class I, II, and III) based on size, deduced amino acid sequence identity, phylogenetic analysis and gene structure. ARFs are ubiquitous among eukaryotes, with a deduced amino acid sequence that is highly conserved across diverse species. They have recently been shown to associate with phospholipid and Golgi membranes in a GTP-dependent manner and are involved in regulating vesicular transport.

Original languageEnglish (US)
Pages (from-to)157-166
Number of pages10
JournalMolecular and Cellular Biochemistry
Volume138
Issue number1-2
DOIs
StatePublished - Dec 1 1994
Externally publishedYes

Keywords

  • adenylyl cyclase
  • ADP-ribosylation factors
  • cholera toxin
  • guanine nucleotide-binding (G) proteins
  • vesicular trafficking

ASJC Scopus subject areas

  • Molecular Biology
  • Genetics
  • Clinical Biochemistry
  • Cell Biology

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