Phosphorylation of lipid metabolic enzymes by yeast Pkc1 protein kinase C requires phosphatidylserine and diacylglycerol.

Protein kinase C in Saccharomyces cerevisiae, i.e., Pkc1, is an enzyme that plays an important role in signal transduction and the regulation of lipid metabolic enzymes. Pkc1 is structurally similar to its counterparts in higher eukaryotes, but its requirement of phosphatidylserine and diacylglycerol for catalytic activity has been unclear. In ...
this work, we examined the role of these lipids in Pkc1 activity with protein and peptide substrates. In agreement with previous findings, yeast Pkc1 did not require phosphatidylserine and diacylglycerol for its activity on the peptide substrates derived from lipid metabolic proteins such as Pah1 (phosphatidate phosphatase), Nem1 (phosphatidate phosphatase phosphatase), and Spo7 (protein phosphatase catalytic subunit). However, the lipids were required for Pkc1 activity on the protein substrates Pah1, Nem1, and Spo7. Compared with diacylglycerol, phosphatidylserine had a greater effect on Pkc1 activity, and its dose-dependent interaction with the protein kinase was shown by the liposome binding assay. The Pkc1-mediated degradation of Pah1 was attenuated in the cho1Δ mutant, which is deficient in phosphatidylserine synthase, supporting the notion that the phospholipid regulates Pkc1 activity in vivo.
J. Lipid Res.
Date: Feb. 02, 2017
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