| http://purl.uniprot.org/citations/12466282 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/12466282 | http://www.w3.org/2000/01/rdf-schema#comment | "Phosducin-like protein (PhLP) is a member of the phosducin family of G-protein betagamma-regulators and exists in two splice variants. The long isoform PhLP(L) and the short isoform PhLP(S) differ by the presence or absence of an 83-amino acid N terminus. In isolated biochemical assay systems, PhLP(L) is the more potent Gbetagamma-inhibitor, whereas the functional role of PhLP(S) is still unclear. We now report that in intact HEK 293 cells, PhLP(S) inhibited Gbetagamma-induced inositol phosphate generation with approximately 20-fold greater potency than PhLP(L). Radiolabeling of transfected HEK 293 cells with [(32)P] revealed that PhLP(L) is constitutively phosphorylated, whereas PhLP(S) is not. Because PhLP(L) has several consensus sites for the constitutively active kinase casein kinase 2 (CK2) in its N terminus, we tested the phosphorylation of the recombinant proteins by either HEK cell cytosol in the presence or absence of kinase inhibitors or by purified CK2. PhLP(L) was a good CK2 substrate, whereas PhLP(S) and phosducin were not. Progressive truncation and serine/threonine to alanine mutations of the PhLP(L) N terminus identified a serine/threonine cluster (Ser-18/Thr-19/Ser-20) within a small N-terminal region of PhLP(L) (amino acids 5-28) as the site in which PhLP(L) function was modified in HEK 293 cells. In native tissue, PhLP(L) also seems to be regulated by phosphorylation because phosphorylated and non-phosphorylated forms of PhLP(L) were detected in mouse brain and adrenal gland. Moreover, the alternatively spliced isoform PhLP(S) was also found in adrenal tissue. Therefore, the physiological control of G-protein regulation by PhLP seems to involve phosphorylation by CK2 and alternative splicing of the regulator."xsd:string |
| http://purl.uniprot.org/citations/12466282 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m206347200"xsd:string |
| http://purl.uniprot.org/citations/12466282 | http://purl.uniprot.org/core/author | "Lohse M.J."xsd:string |
| http://purl.uniprot.org/citations/12466282 | http://purl.uniprot.org/core/author | "Quitterer U."xsd:string |
| http://purl.uniprot.org/citations/12466282 | http://purl.uniprot.org/core/author | "Bermel C."xsd:string |
| http://purl.uniprot.org/citations/12466282 | http://purl.uniprot.org/core/author | "Grubel T."xsd:string |
| http://purl.uniprot.org/citations/12466282 | http://purl.uniprot.org/core/author | "Humrich J."xsd:string |
| http://purl.uniprot.org/citations/12466282 | http://purl.uniprot.org/core/date | "2003"xsd:gYear |
| http://purl.uniprot.org/citations/12466282 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
| http://purl.uniprot.org/citations/12466282 | http://purl.uniprot.org/core/pages | "4474-4481"xsd:string |
| http://purl.uniprot.org/citations/12466282 | http://purl.uniprot.org/core/title | "Regulation of phosducin-like protein by casein kinase 2 and N-terminal splicing."xsd:string |
| http://purl.uniprot.org/citations/12466282 | http://purl.uniprot.org/core/volume | "278"xsd:string |
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