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J. Biol. Chem., Vol. 264, Issue 34, 20167-20170, 12, 1989
UH Kim, JW Kim and SG Rhee
The mechanism by which cAMP modulates the activity of phosphoinositide-
specific phospholipase C (PLC) was studied. Elevation of cAMP inhibited
both basal and norepinephrine-stimulated phosphoinositide breakdown in
C6Bu1 cells which contain at least three PLC isozymes, PLC-beta, PLC-
gamma, and PLC-delta. Treatment of C6Bu1 cells with cAMP-elevating agents
(cholera toxin, isobutylmethylxanthine, forskolin, and 8-bromo- cAMP)
increased serine phosphate in PLC-gamma, but the phosphate contents in
PLC-beta and PLC-delta were not changed. In addition, cAMP- dependent
protein kinase selectively phosphorylated purified PLC-gamma among the
three isozymes and added a single phosphate at serine. The serine
phosphorylation, nevertheless, did not affect the activity of PLC-gamma in
vitro. We propose, therefore, that the phosphorylation of PLC-gamma by
cAMP-dependent protein kinase alters its interaction with putative
modulatory proteins and leads to its inhibition.
Phosphorylation of phospholipase C-gamma by cAMP-dependent protein kinase
Laboratory of Biochemistry, National Heart, Lung, and Blood Institute, Bethesda, Maryland 20892.
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