Emerging Roles for RGS Proteins in Cell Signalling

Trends Pharmacol Sci. 1999 Sep;20(9):376-82. doi: 10.1016/s0165-6147(99)01369-3.

Abstract

Regulators of G-protein signalling (RGS proteins) are a family of highly diverse, multifunctional signalling proteins that share a conserved 120 amino acid domain (RGS domain). RGS domains bind directly to activated Galpha subunits and act as GTPase-activating proteins (GAPs) to attenuate and/or modulate hormone and neurotransmitter receptor-initiated signalling by both Galpha-GTP and Gbetagamma. Apart from this structural domain, which is shared by all known RGS proteins, these proteins differ widely in their overall size and amino acid identity and possess a remarkable variety of structural domains and motifs. These biochemical features impart signalling functions and/or enable RGS proteins to interact with a growing list of unexpected protein-binding partners with diverse cellular roles. New appreciation for the broader cellular functions of RGS proteins challenges established models of G-protein signalling and serves to identify these proteins as central participants in receptor signalling and cell physiology.

Publication types

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

MeSH terms

  • Animals
  • GTP-Binding Proteins / chemistry
  • GTP-Binding Proteins / physiology*
  • Hormones / physiology
  • Humans
  • Neurotransmitter Agents / physiology
  • Proteins / physiology*
  • RGS Proteins*
  • Receptors, Cell Surface / drug effects
  • Signal Transduction*

Substances

  • Hormones
  • Neurotransmitter Agents
  • Proteins
  • RGS Proteins
  • RGS12 protein, human
  • Receptors, Cell Surface
  • Rgs2 protein, mouse
  • GTP-Binding Proteins