| http://purl.uniprot.org/citations/12217858 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/12217858 | http://www.w3.org/2000/01/rdf-schema#comment | "We purified His-tagged ROMK1 and carried out in vitro phosphorylation assays with (32)P-radiolabeled ATP to determine whether ROMK1 protein is a substrate for PTK. Addition of active c-Src and [(32)P]ATP to the purified ROMK1 protein resulted in the phosphorylation of the ROMK1 protein. However, c-Src did not phosphorylate R1Y337A in which tyrosine residue 337 was mutated to alanine. Furthermore, phosphopeptide mapping identified two phosphopeptides from the trypsin-digested ROMK1 protein. In contrast, no phosphorylated peptide has been found in the trypsin-digested R1Y337A protein. This suggested that two phosphorylated peptides might contain the same tyrosine residue. Also, addition of c-Src and [(32)P]ATP phosphorylated the synthesized peptide corresponding to amino acid sequence 333-362 of the COOH terminus of ROMK1. We then examined the effect of dietary K intake on the tyrosine-phosphorylated ROMK level. Although the ROMK channels pulled down by immunoprecipitation with ROMK antibody were the same from rats on a K-deficient diet or on a high-K diet, more ROMK channels were phosphorylated by PTK in rats on a K-deficient diet than those on a high-K diet. We conclude that ROMK1 can be phosphorylated by PTK and that tyrosine residue 337 is the key site for the phosphorylation. Also, the tyrosine phosphorylation of ROMK is modulated by dietary K intake. This strongly suggests that PTK is an important member of the aldosterone-independent signal transduction pathway for regulating renal K secretion."xsd:string |
| http://purl.uniprot.org/citations/12217858 | http://purl.org/dc/terms/identifier | "doi:10.1152/ajprenal.00160.2002"xsd:string |
| http://purl.uniprot.org/citations/12217858 | http://purl.uniprot.org/core/author | "Jin L."xsd:string |
| http://purl.uniprot.org/citations/12217858 | http://purl.uniprot.org/core/author | "Wang W.H."xsd:string |
| http://purl.uniprot.org/citations/12217858 | http://purl.uniprot.org/core/author | "Lin D.H."xsd:string |
| http://purl.uniprot.org/citations/12217858 | http://purl.uniprot.org/core/author | "Lerea K.M."xsd:string |
| http://purl.uniprot.org/citations/12217858 | http://purl.uniprot.org/core/author | "Sterling H."xsd:string |
| http://purl.uniprot.org/citations/12217858 | http://purl.uniprot.org/core/author | "Giebisch G."xsd:string |
| http://purl.uniprot.org/citations/12217858 | http://purl.uniprot.org/core/author | "Welling P."xsd:string |
| http://purl.uniprot.org/citations/12217858 | http://purl.uniprot.org/core/date | "2002"xsd:gYear |
| http://purl.uniprot.org/citations/12217858 | http://purl.uniprot.org/core/name | "Am J Physiol Renal Physiol"xsd:string |
| http://purl.uniprot.org/citations/12217858 | http://purl.uniprot.org/core/pages | "F671-7"xsd:string |
| http://purl.uniprot.org/citations/12217858 | http://purl.uniprot.org/core/title | "K depletion increases protein tyrosine kinase-mediated phosphorylation of ROMK."xsd:string |
| http://purl.uniprot.org/citations/12217858 | http://purl.uniprot.org/core/volume | "283"xsd:string |
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