Interaction of the G-protein G11alpha with receptors and phosphoinositidase C: the contribution of G-protein palmitoylation and membrane association

FEBS Lett. 1997 May 5;407(3):257-60. doi: 10.1016/s0014-5793(97)00300-1.

Abstract

Wild-type and palmitoylation defective mutants of the murine G protein G11alpha were transfected into HEK293 cells. Wild-type G11alpha was membrane associated, Cys9Ser Cys10Ser G11alpha was present in the soluble fraction whilst both Cys9Ser G11alpha and Cys10Ser G11alpha were distributed between the fractions. Expression of the rat TRH receptor resulted in agonist stimulation of inositol phosphate accumulation. The degree of stimulation produced by TRH following co-transfection of the palmitoylation-resistant forms of G11alpha compared to the wild-type protein correlated with the amount of membrane-associated G protein.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cell Line
  • Enzyme Activation / drug effects
  • GTP-Binding Proteins / chemistry
  • GTP-Binding Proteins / genetics
  • GTP-Binding Proteins / metabolism*
  • Humans
  • Mice
  • Mutation
  • Palmitic Acids / chemistry
  • Palmitic Acids / metabolism
  • Phosphoric Diester Hydrolases / metabolism*
  • Rats
  • Receptors, Thyrotropin-Releasing Hormone / drug effects
  • Receptors, Thyrotropin-Releasing Hormone / genetics
  • Receptors, Thyrotropin-Releasing Hormone / metabolism*
  • Thyrotropin-Releasing Hormone / pharmacology
  • Transfection

Substances

  • Palmitic Acids
  • Receptors, Thyrotropin-Releasing Hormone
  • Thyrotropin-Releasing Hormone
  • Phosphoric Diester Hydrolases
  • glycerophosphoinositol glycerophosphodiesterase
  • GTP-Binding Proteins