| http://purl.uniprot.org/citations/24876385 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/24876385 | http://www.w3.org/2000/01/rdf-schema#comment | "Yeast Pah1p is the phosphatidate phosphatase that catalyzes the penultimate step in triacylglycerol synthesis and plays a role in the transcriptional regulation of phospholipid synthesis genes. The enzyme is multiply phosphorylated, some of which is mediated by Pho85p-Pho80p, Cdc28p-cyclin B, and protein kinase A. Here, we showed that Pah1p is a bona fide substrate of protein kinase C; the phosphorylation reaction was time- and dose-dependent and dependent on the concentrations of ATP (Km = 4.5 μm) and Pah1p (Km = 0.75 μm). The stoichiometry of the reaction was 0.8 mol of phosphate/mol of Pah1p. By combining mass spectrometry, truncation analysis, site-directed mutagenesis, and phosphopeptide mapping, we identified Ser-677, Ser-769, Ser-773, and Ser-788 as major sites of phosphorylation. Analysis of Pah1p phosphorylations by different protein kinases showed that prephosphorylation with protein kinase C reduces its subsequent phosphorylation with protein kinase A and vice versa. Prephosphorylation with Pho85p-Pho80p had an inhibitory effect on its subsequent phosphorylation with protein kinase C; however, prephosphorylation with protein kinase C had no effect on the subsequent phosphorylation with Pho85p-Pho80p. Unlike its phosphorylations by Pho85p-Pho80p and protein kinase A, which cause a significant reduction in phosphatidate phosphatase activity, the phosphorylation of Pah1p by protein kinase C had a small stimulatory effect on the enzyme activity. Analysis of phosphorylation-deficient forms of Pah1p indicated that protein kinase C does not have a major effect on its location or its function in triacylglycerol synthesis, but instead, the phosphorylation favors loss of Pah1p abundance when it is not phosphorylated with Pho85p-Pho80p."xsd:string |
| http://purl.uniprot.org/citations/24876385 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m114.581462"xsd:string |
| http://purl.uniprot.org/citations/24876385 | http://purl.uniprot.org/core/author | "Carman G.M."xsd:string |
| http://purl.uniprot.org/citations/24876385 | http://purl.uniprot.org/core/author | "Han G.S."xsd:string |
| http://purl.uniprot.org/citations/24876385 | http://purl.uniprot.org/core/author | "Su W.M."xsd:string |
| http://purl.uniprot.org/citations/24876385 | http://purl.uniprot.org/core/date | "2014"xsd:gYear |
| http://purl.uniprot.org/citations/24876385 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
| http://purl.uniprot.org/citations/24876385 | http://purl.uniprot.org/core/pages | "18818-18830"xsd:string |
| http://purl.uniprot.org/citations/24876385 | http://purl.uniprot.org/core/title | "Cross-talk phosphorylations by protein kinase C and Pho85p-Pho80p protein kinase regulate Pah1p phosphatidate phosphatase abundance in Saccharomyces cerevisiae."xsd:string |
| http://purl.uniprot.org/citations/24876385 | http://purl.uniprot.org/core/volume | "289"xsd:string |
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