Interaction of the G-protein G 11α with receptors and phosphoinositidase C: : The contribution of G-protein palmitoylation and membrane association

Abstract

Wild-type and palmitoylation defective mutants of the murine G protein G 11α were transfected into HEK293 cells. Wild-type G 11α was membrane associated, Cys9Ser Cys10Ser G 11α was present in the soluble fraction whilst both Cys9Ser G 11α and Cys10Ser G 11α 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 G 11α compared to the wild-type protein correlated with the amount of membrane-associated G protein.