Arf GAPs as regulators of the actin cytoskeleton

Biol Cell. 2007 Oct;99(10):583-600. doi: 10.1042/bc20070034.


The Arf (ADP-ribosylation factor) GAPs (GTPase-activating proteins) are a family of proteins with a common catalytic domain that induces hydrolysis of GTP bound to Arf GTP-binding proteins. At least three groups of multidomain Arf GAPs affect the actin cytoskeleton and cellular activities, such as migration and movement, that depend on the cytoskeleton. One role of the Arf GAPs is to regulate membrane remodelling that accompanies actin polymerization. Regulation of membrane remodelling is mediated in part by the regulation of Arf proteins. However, Arf GAPs also regulate actin independently of effects on membranes or Arf. These functions include acting as upstream regulators of Rho family proteins and providing a scaffold for Rho effectors and exchange factors. With multiple functional elements, the Arf GAPs could integrate signals and biochemical activities that result in co-ordinated changes in actin and membranes necessary for a wide range of cellular functions.

Publication types

  • Research Support, N.I.H., Intramural
  • Review

MeSH terms

  • ADP-Ribosylation Factors / genetics
  • ADP-Ribosylation Factors / metabolism*
  • Actins / metabolism*
  • Adaptor Proteins, Signal Transducing / metabolism
  • Animals
  • Carrier Proteins / metabolism
  • Cell Line
  • Cytoskeleton / metabolism*
  • Cytoskeleton / ultrastructure
  • GTPase-Activating Proteins / genetics
  • GTPase-Activating Proteins / metabolism*
  • Humans
  • Neurons / cytology
  • Neurons / metabolism
  • Paxillin / metabolism
  • Signal Transduction / physiology
  • Substrate Specificity
  • rho GTP-Binding Proteins / metabolism


  • ARAP2 protein, human
  • Actins
  • Adaptor Proteins, Signal Transducing
  • Asap1 protein, mouse
  • Carrier Proteins
  • GTPase-Activating Proteins
  • Paxillin
  • ADP-Ribosylation Factors
  • rho GTP-Binding Proteins