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• W2079358631 endingPage "1498" @default.
• W2079358631 startingPage "1486" @default.
• W2079358631 abstract "The Saccharomyces cerevisiae PAH1-encoded phosphatidate phosphatase (PAP) catalyzes the penultimate step in the synthesis of triacylglycerol and plays a role in the transcriptional regulation of phospholipid synthesis genes. PAP is phosphorylated at multiple Ser and Thr residues and is dephosphorylated for in vivo function by the Nem1p-Spo7p protein phosphatase complex localized in the nuclear/endoplasmic reticulum membrane. In this work, we characterized seven previously identified phosphorylation sites of PAP that are within the Ser/Thr-Pro motif. When expressed on a low copy plasmid, wild type PAP could not complement the pah1Δ mutant in the absence of the Nem1p-Spo7p complex. However, phosphorylation-deficient PAP (PAP-7A) containing alanine substitutions for the seven phosphorylation sites bypassed the requirement of the phosphatase complex and complemented the pah1Δ nem1Δ mutant phenotypes, such as temperature sensitivity, nuclear/endoplasmic reticulum membrane expansion, decreased triacylglycerol synthesis, and derepression of INO1 expression. Subcellular fractionation coupled with immunoblot analysis showed that PAP-7A was highly enriched in the membrane fraction. In fluorescence spectroscopy analysis, the PAP-7A showed tighter association with phospholipid vesicles than wild type PAP. Using site-directed mutagenesis of PAP, we identified Ser(602), Thr(723), and Ser(744), which belong to the seven phosphorylation sites, as the sites phosphorylated by the CDC28 (CDK1)-encoded cyclin-dependent kinase. Compared with the dephosphorylation mimic of the seven phosphorylation sites, alanine substitution for Ser(602), Thr(723), and/or Ser(744) had a partial effect on circumventing the requirement for the Nem1p-Spo7p complex." @default.
• W2079358631 created "2016-06-24" @default.
• W2079358631 creator A5015880535 @default.
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• W2079358631 creator A5088882066 @default.
• W2079358631 date "2011-01-01" @default.
• W2079358631 modified "2023-10-01" @default.
• W2079358631 title "Phosphorylation of Phosphatidate Phosphatase Regulates Its Membrane Association and Physiological Functions in Saccharomyces cerevisiae" @default.
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• W2079358631 doi "https://doi.org/10.1074/jbc.m110.155598" @default.
• W2079358631 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3020757" @default.
• W2079358631 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/21081492" @default.
• W2079358631 hasPublicationYear "2011" @default.
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