RGS Proteins: More Than Just GAPs for Heterotrimeric G Proteins

Trends Cell Biol. 1999 Apr;9(4):138-44. doi: 10.1016/s0962-8924(99)01515-9.

Abstract

Members of the newly described RGS family of proteins have a common RGS domain that contains GTPase-activating activity for many Galpha subunits of heterotrimeric G proteins. Their ability to dampen signalling via Galphai-, Galphaq- and Galpha12/13-coupled pathways makes them crucial players in mediating the multitude of cellular processes controlled by heterotrimeric G proteins. Some RGS proteins also contain additional motifs that link them to other signalling networks, where they constitute effector-type molecules. This review summarizes recent findings on RGS proteins, especially those that implicate RGS proteins in more than just enhancing the GTPase activity of their Galpha subunit targets.

Publication types

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

MeSH terms

  • Adaptor Proteins, Signal Transducing
  • Animals
  • Chemical Phenomena
  • Chemistry, Physical
  • Dishevelled Proteins
  • Drosophila melanogaster / metabolism
  • GTP Phosphohydrolases / metabolism*
  • GTP-Binding Proteins / physiology*
  • GTPase-Activating Proteins
  • Macromolecular Substances
  • Mammals / metabolism
  • Membrane Proteins / metabolism
  • Models, Biological
  • Multigene Family
  • Organ Specificity
  • Phosphoproteins / physiology
  • Protein Conformation
  • Proteins / classification
  • Proteins / physiology*
  • Rats
  • Signal Transduction / physiology*
  • Structure-Activity Relationship
  • Subcellular Fractions / metabolism
  • Transcription, Genetic

Substances

  • Adaptor Proteins, Signal Transducing
  • Dishevelled Proteins
  • GTPase-Activating Proteins
  • Macromolecular Substances
  • Membrane Proteins
  • Phosphoproteins
  • Proteins
  • GTP Phosphohydrolases
  • GTP-Binding Proteins