Structural heterogeneity of membrane receptors and GTP-binding proteins and its functional consequences for signal transduction

Eur J Biochem. 1991 Jul 1;199(1):1-15. doi: 10.1111/j.1432-1033.1991.tb16085.x.

Abstract

Recent information obtained, mainly by recombinant cDNA technology, on structural heterogeneity of hormone and transmitter receptors, of GTP-binding proteins (G-proteins) and, especially, of G-protein-linked receptors is reviewed and the implications of structural heterogeneity for diversity of hormone and transmitter actions is discussed. For the future, three-dimensional structural analysis of membrane proteins participating in signal transmission and transduction pathways is needed in order to understand the molecular basis of allosteric regulatory mechanisms governing the interactions between these proteins including hysteretic properties and cell-cybernetic aspects.

Publication types

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

MeSH terms

  • Acetylcholine / metabolism
  • Adenylyl Cyclases / metabolism
  • Animals
  • Cell Membrane / metabolism*
  • GTP-Binding Proteins / metabolism*
  • Membrane Proteins / metabolism
  • Protein Conformation
  • Receptors, Adrenergic, alpha / metabolism
  • Signal Transduction*
  • Turkeys

Substances

  • Membrane Proteins
  • Receptors, Adrenergic, alpha
  • GTP-Binding Proteins
  • Adenylyl Cyclases
  • Acetylcholine