Identification of a Gs-protein coupling domain to the beta-adrenoceptor using site-specific synthetic peptides. Carboxyl terminus of Gs alpha is involved in coupling to beta-adrenoceptors

FEBS Lett. 1990 Feb 26;261(2):294-8. doi: 10.1016/0014-5793(90)80575-4.


Competition between Gs-protein and the synthetic peptide, GSA 379-394, derived from the carboxyl-terminal region of the alpha s-subunit, led to complete inhibition of receptor-mediated adenylate cyclase activation in turkey erythrocyte membranes. Related peptides corresponding to the homologous carboxyl-terminal region of alpha t-, alpha il- or alpha o-subunits did not interfere with beta-receptor-Gs coupling. The direct coupling between Gs and adenylate cyclase was not influenced by any of these peptides. These results emphasize the important role of the carboxyl-terminus of G-protein alpha-subunits for the specific recognition of their corresponding receptors and for signal transduction.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenylyl Cyclases / blood
  • Amino Acid Sequence
  • Animals
  • Antibodies / pharmacology
  • Binding Sites
  • Binding, Competitive
  • Enzyme Activation
  • Erythrocyte Membrane / enzymology
  • GTP-Binding Proteins / immunology
  • GTP-Binding Proteins / metabolism*
  • Molecular Sequence Data
  • Peptide Fragments / immunology
  • Peptide Fragments / metabolism
  • Receptors, Adrenergic, beta / metabolism*
  • Signal Transduction
  • Turkeys


  • Antibodies
  • Peptide Fragments
  • Receptors, Adrenergic, beta
  • GTP-Binding Proteins
  • Adenylyl Cyclases