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Phosphorylation of yeast phosphatidate phosphatase by protein kinase C

The yeast PAH1‐encoded phosphatidate (PA) phosphatase, which catalyzes the Mg2+‐dependent dephosphorylation of PA to yield diacylglycerol, plays a major role in the regulation of lipid metabolism. In fact, mutants defective in the enzyme show defects in phospholipid synthesis regulation, an abnormal expansion of the nuclear/ER membrane, and a 90 % reduction in triacylglycerol. PA phosphatase has been identified as a phosphoprotein in vivo. Studies with recombinant enzyme isolated from Escherichia coli have shown that PA phosphatase is a substrate for protein kinase C. Truncation analysis of PA phosphatase followed by site‐directed mutagenesis experiments revealed that Ser677, Ser769, and Ser788 are the major sites for protein kinase C phosphorylation in vitro. Yeast cells that carry a S677A S769A S788A triple mutation in PA phosphatase exhibit a 40 % reduction in enzyme phosphorylation. These results indicated that protein kinase C phosphorylates PA phosphatase in vivo. Supported by NIH grant GM 50679.