Receptor-effector coupling by G proteins

Biochim Biophys Acta. 1990 May 7;1031(2):163-224. doi: 10.1016/0304-4157(90)90007-y.


The primary structure of G proteins as deduced from purified proteins and cloned subunits is presented. When known, their functions are discussed, as are recent data on direct regulation of ionic channels by G proteins. Experiments on expression of alpha subunits, either in bacteria or by in vitro translation of mRNA synthesized from cDNA are presented as tools for definitive assignment of function to a given G protein. The dynamics of G protein-mediated signal transduction are discussed. Key points include the existence of two superimposed regulatory cycles in which upon activation by GTP, G proteins dissociate into alpha and beta gamma and their dissociated alpha subunits hydrolyze GTP. The action of receptors to catalyze rather than regulate by allostery the activation of G proteins by GTP is emphasized, as is the role of subunit dissociation, without which receptors could not act as catalysts. To facilitate the reading of this review, we have presented the various subtopics of this rapidly expanding field in sections 1-1X, each of which is organized as a self-contained sub-chapter that can be read independently of the others.

Publication types

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

MeSH terms

  • Amino Acid Sequence
  • Animals
  • GTP-Binding Proteins / physiology*
  • Guanosine Triphosphate / metabolism
  • Guanosine Triphosphate / physiology
  • Humans
  • Ion Channel Gating / physiology*
  • Molecular Sequence Data
  • Protein Conformation
  • Receptors, Cell Surface / physiology*
  • Recombinant Proteins / biosynthesis
  • Signal Transduction / physiology*
  • Structure-Activity Relationship


  • Receptors, Cell Surface
  • Recombinant Proteins
  • Guanosine Triphosphate
  • GTP-Binding Proteins