| http://purl.uniprot.org/citations/27044741 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/27044741 | http://www.w3.org/2000/01/rdf-schema#comment | "Pah1 phosphatidate phosphatase in Saccharomyces cerevisiae catalyzes the penultimate step in the synthesis of triacylglycerol (i.e. the production of diacylglycerol by dephosphorylation of phosphatidate). The enzyme playing a major role in lipid metabolism is subject to phosphorylation (e.g. by Pho85-Pho80, Cdc28-cyclin B, and protein kinases A and C) and dephosphorylation (e.g. by Nem1-Spo7) that regulate its cellular location, catalytic activity, and stability/degradation. In this work, we show that Pah1 is a substrate for casein kinase II (CKII); its phosphorylation was time- and dose-dependent and was dependent on the concentrations of Pah1 (Km = 0.23 μm) and ATP (Km = 5.5 μm). By mass spectrometry, truncation analysis, site-directed mutagenesis, phosphopeptide mapping, and phosphoamino acid analysis, we identified that >90% of its phosphorylation occurs on Thr-170, Ser-250, Ser-313, Ser-705, Ser-814, and Ser-818. The CKII-phosphorylated Pah1 was a substrate for the Nem1-Spo7 protein phosphatase and was degraded by the 20S proteasome. The prephosphorylation of Pah1 by protein kinase A or protein kinase C reduced its subsequent phosphorylation by CKII. The prephosphorylation of Pah1 by CKII reduced its subsequent phosphorylation by protein kinase A but not by protein kinase C. The expression of Pah1 with combined mutations of S705D and 7A, which mimic its phosphorylation by CKII and lack of phosphorylation by Pho85-Pho80, caused an increase in triacylglycerol content and lipid droplet number in cells expressing the Nem1-Spo7 phosphatase complex."xsd:string |
| http://purl.uniprot.org/citations/27044741 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m116.726588"xsd:string |
| http://purl.uniprot.org/citations/27044741 | http://purl.uniprot.org/core/author | "Carman G.M."xsd:string |
| http://purl.uniprot.org/citations/27044741 | http://purl.uniprot.org/core/author | "Han G.S."xsd:string |
| http://purl.uniprot.org/citations/27044741 | http://purl.uniprot.org/core/author | "Hsieh L.S."xsd:string |
| http://purl.uniprot.org/citations/27044741 | http://purl.uniprot.org/core/author | "Su W.M."xsd:string |
| http://purl.uniprot.org/citations/27044741 | http://purl.uniprot.org/core/date | "2016"xsd:gYear |
| http://purl.uniprot.org/citations/27044741 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
| http://purl.uniprot.org/citations/27044741 | http://purl.uniprot.org/core/pages | "9974-9990"xsd:string |
| http://purl.uniprot.org/citations/27044741 | http://purl.uniprot.org/core/title | "Phosphorylation of Yeast Pah1 Phosphatidate Phosphatase by Casein Kinase II Regulates Its Function in Lipid Metabolism."xsd:string |
| http://purl.uniprot.org/citations/27044741 | http://purl.uniprot.org/core/volume | "291"xsd:string |
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