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J Biol Chem, Vol. 273, Issue 29, 18023-18027, July 17, 1998

Phosphorylation of Serine 1105 by Protein Kinase A Inhibits Phospholipase C₃ Stimulation by G_q

Caiping Yue, Kimberly L. Dodge, Günther Weber^§, and Barbara M. Sanborn

From the  Department of Biochemistry and Molecular Biology, University of Texas Houston Medical School, Houston, Texas 77225 and the ^§ Department of Molecular Medicine, Clinical Genetics Unit, CMM, L8:02, Karolinska Hospital, S-17176 Stockholm, Sweden

The mechanism by which protein kinase A (PKA) inhibits G_q-stimulated phospholipase C activity of the  subclass (PLC) is unknown. We present evidence that phosphorylation of PLC₃ by PKA results in inhibition of G_q-stimulated PLC₃ activity, and we identify the site of phosphorylation. Two-dimensional phosphoamino acid analysis of in vitro phosphorylated PLC₃ revealed a single phosphoserine as the putative PKA site, and peptide mapping yielded one phosphopeptide. The residue was identified as Ser¹¹⁰⁵ by direct sequencing of reverse-phase high pressure liquid chromatography-isolated phosphopeptide and by site-directed mutagenesis. Overexpression of G_q with PLC₃ or PLC₃ (Ser¹¹⁰⁵  Ala) mutant in COSM6 cells resulted in a 5-fold increase in [³H]phosphatidylinositol 1,4,5-trisphosphate formation compared with expression of G_q, PLC₃, or PLC₃ (Ser¹¹⁰⁵  Ala) mutant alone. Whereas G_q-stimulated PLC₃ activity was inhibited by 58-71% by overexpression of PKA catalytic subunit, G_q-stimulated PLC₃ (Ser¹¹⁰⁵  Ala) mutant activity was not affected. Furthermore, phosphatidylinositide turnover stimulated by presumably G_q-coupled M1 muscarinic and oxytocin receptors was completely inhibited by pretreating cells with 8-[4-chlorophenythio]-cAMP in RBL-2H3 cells expressing only PLC₃. These data establish that direct phosphorylation by PKA of Ser¹¹⁰⁵ in the putative G-box of PLC₃ inhibits G_q-stimulated PLC₃ activity. This can at least partially explain the inhibitory effect of PKA on G_q-stimulated phosphatidylinositide turnover observed in a variety of cells and tissues.

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