Mutation of glycine 49 to valine in the alpha subunit of GS results in the constitutive elevation of cyclic AMP synthesis

Biochemistry. 1989 May 30;28(11):4547-51. doi: 10.1021/bi00437a006.

Abstract

The G-protein GS couples hormone-activated receptors with adenylyl cyclase and stimulates increased cyclic AMP synthesis. Transient expression in COS-1 cells of cDNAs coding for the GS alpha-subunit (alpha S) or alpha S cDNAs having single amino acid mutations Gly49----Val or Gly225----Thr elevated cyclic AMP levels, resulting in the activation of cyclic AMP dependent protein kinase. Stable expression in Chinese hamster ovary cells of alpha S Val49 cDNA resulted in a small constitutive elevation of cyclic AMP that was sufficient to persistently activate cyclic AMP dependent protein kinase activity 1.5-2-fold over basal activity. Stable expression of wild-type alpha S or alpha S Thr225 in Chinese hamster ovary cells was less effective in sustaining elevated cyclic AMP synthesis and kinase activation compared to alpha SVal49.

Publication types

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

MeSH terms

  • Animals
  • Cell Line
  • Cricetinae
  • Cricetulus
  • Cyclic AMP / biosynthesis*
  • DNA / analysis
  • Enzyme Activation
  • Female
  • GTP-Binding Proteins / genetics*
  • GTP-Binding Proteins / metabolism
  • Glycine / genetics*
  • Glycine / metabolism
  • Mutation
  • Plasmids
  • Protein Kinases / metabolism
  • Transfection
  • Valine / genetics*
  • Valine / metabolism

Substances

  • DNA
  • Cyclic AMP
  • Protein Kinases
  • GTP-Binding Proteins
  • Valine
  • Glycine