| http://purl.uniprot.org/citations/31645435 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/31645435 | http://www.w3.org/2000/01/rdf-schema#comment | "The PAH1-encoded phosphatidate phosphatase in Saccharomyces cerevisiae plays a major role in triacylglycerol synthesis and the control of phospholipid synthesis. For its catalytic function on the nuclear/endoplasmic reticulum membrane, Pah1 translocates to the membrane through its phosphorylation/dephosphorylation. Pah1 phosphorylation on multiple serine/threonine residues is complex and catalyzed by diverse protein kinases. In this work, we demonstrate that Pah1 is phosphorylated by the YCK1-encoded casein kinase I (CKI), regulating Pah1 catalytic activity and phosphorylation. Phosphoamino acid analysis coupled with phosphopeptide mapping of the CKI-phosphorylated Pah1 indicated that it is phosphorylated mainly on multiple serine residues. Using site-directed mutagenesis and phosphorylation analysis of Pah1, we identified eight serine residues (i.e. Ser-114, Ser-475, Ser-511, Ser-602, Ser-677, Ser-705, Ser-748, and Ser-774) as the target sites of CKI. Of these residues, Ser-475 and Ser-511 were specific for CKI, whereas the others were shared by casein kinase II (Ser-705), Cdc28-cyclin B (Ser-602), Pho85-Pho80 (Ser-114, Ser-602, and Ser-748), protein kinase A (Ser-667 and Ser-774), and protein kinase C (Ser-677). CKI-mediated phosphorylation of Pah1 stimulated both its phosphatidate phosphatase activity and its subsequent phosphorylation by casein kinase II. However, the CKI-mediated phosphorylation of Pah1 strongly inhibited its subsequent phosphorylation by Pho85-Pho80, protein kinase A, and protein kinase C. In a reciprocal analysis, Pah1 phosphorylation by Pho85-Pho80 inhibited subsequent phosphorylation by CKI. CKI-mediated Pah1 phosphorylation was also inhibited by a peptide containing the Pah1 residues 506-517, including the kinase-specific Ser-511 residue. These findings advance our understanding of how Pah1 catalytic activity and phosphorylation are regulated by multiple protein kinases."xsd:string |
| http://purl.uniprot.org/citations/31645435 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.ra119.011314"xsd:string |
| http://purl.uniprot.org/citations/31645435 | http://purl.uniprot.org/core/author | "Carman G.M."xsd:string |
| http://purl.uniprot.org/citations/31645435 | http://purl.uniprot.org/core/author | "Han G.S."xsd:string |
| http://purl.uniprot.org/citations/31645435 | http://purl.uniprot.org/core/author | "Hsieh L.S."xsd:string |
| http://purl.uniprot.org/citations/31645435 | http://purl.uniprot.org/core/author | "Hassaninasab A."xsd:string |
| http://purl.uniprot.org/citations/31645435 | http://purl.uniprot.org/core/author | "Su W.M."xsd:string |
| http://purl.uniprot.org/citations/31645435 | http://purl.uniprot.org/core/date | "2019"xsd:gYear |
| http://purl.uniprot.org/citations/31645435 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
| http://purl.uniprot.org/citations/31645435 | http://purl.uniprot.org/core/pages | "18256-18268"xsd:string |
| http://purl.uniprot.org/citations/31645435 | http://purl.uniprot.org/core/title | "Yck1 casein kinase I regulates the activity and phosphorylation of Pah1 phosphatidate phosphatase from Saccharomyces cerevisiae."xsd:string |
| http://purl.uniprot.org/citations/31645435 | http://purl.uniprot.org/core/volume | "294"xsd:string |
| http://purl.uniprot.org/citations/31645435 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/31645435 |
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