| http://purl.uniprot.org/citations/17363702 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/17363702 | http://www.w3.org/2000/01/rdf-schema#comment | "Heterotrimeric G proteins are pivotal regulators of myocardial contractility. In addition to the receptor-induced GDP/GTP exchange, G protein alpha subunits can be activated by a phosphate transfer via a plasma membrane-associated complex of nucleoside diphosphate kinase B (NDPK B) and G protein betagamma-dimers (Gbetagamma). To investigate the physiological role of this phosphate transfer in cardiomyocytes, we generated a Gbeta1gamma2-dimer carrying a single amino acid exchange at the intermediately phosphorylated His-266 in the beta1 subunit (Gbeta1H266Lgamma2). Recombinantly expressed Gbeta1H266Lgamma2 were integrated into heterotrimeric G proteins in rat cardiomyocytes but were deficient in intermediate Gbeta phosphorylation. Compared with wild-type Gbeta1gamma2 (Gbeta1WTgamma2), overexpression of Gbeta1H266Lgamma2 suppressed basal cAMP formation up to 55%. A similar decrease in basal cAMP production occurred when the formation of NDPK B/Gbetagamma complexes was attenuated by siRNA-mediated NDPK B knockdown. In adult rat cardiomyocytes expressing Gbeta1H266Lgamma2, the basal contractility was suppressed by approximately 50% which correlated to similarly reduced basal cAMP levels and reduced Ser16-phosphorylation of phospholamban. In the presence of the beta-adrenoceptor agonist isoproterenol, the total cAMP formation and contractility were significantly lower in Gbeta1H266Lgamma2 than in Gbeta1WTgamma2 expressing cardiomyocytes. However, the relative isoproterenol-induced increased was not affected by Gbeta1H266Lgamma2. We conclude that the receptor-independent activation of G proteins via NDPK B/Gbetagamma complexes requires the intermediate phosphorylation of G protein beta subunits at His-266. Our results highlight the histidine kinase activity of NDPK B for Gbeta and demonstrate its contribution to the receptor-independent regulation of cAMP synthesis and contractility in intact cardiomyocytes."xsd:string |
| http://purl.uniprot.org/citations/17363702 | http://purl.org/dc/terms/identifier | "doi:10.1161/01.res.0000264058.28808.cc"xsd:string |
| http://purl.uniprot.org/citations/17363702 | http://purl.uniprot.org/core/author | "Lutz S."xsd:string |
| http://purl.uniprot.org/citations/17363702 | http://purl.uniprot.org/core/author | "Wieland T."xsd:string |
| http://purl.uniprot.org/citations/17363702 | http://purl.uniprot.org/core/author | "Frey N."xsd:string |
| http://purl.uniprot.org/citations/17363702 | http://purl.uniprot.org/core/author | "Katus H.A."xsd:string |
| http://purl.uniprot.org/citations/17363702 | http://purl.uniprot.org/core/author | "Koehler H."xsd:string |
| http://purl.uniprot.org/citations/17363702 | http://purl.uniprot.org/core/author | "Eschenhagen T."xsd:string |
| http://purl.uniprot.org/citations/17363702 | http://purl.uniprot.org/core/author | "Niroomand F."xsd:string |
| http://purl.uniprot.org/citations/17363702 | http://purl.uniprot.org/core/author | "Luedde M."xsd:string |
| http://purl.uniprot.org/citations/17363702 | http://purl.uniprot.org/core/author | "Hippe H.J."xsd:string |
| http://purl.uniprot.org/citations/17363702 | http://purl.uniprot.org/core/date | "2007"xsd:gYear |
| http://purl.uniprot.org/citations/17363702 | http://purl.uniprot.org/core/name | "Circ Res"xsd:string |
| http://purl.uniprot.org/citations/17363702 | http://purl.uniprot.org/core/pages | "1191-1199"xsd:string |
| http://purl.uniprot.org/citations/17363702 | http://purl.uniprot.org/core/title | "Regulation of cardiac cAMP synthesis and contractility by nucleoside diphosphate kinase B/G protein beta gamma dimer complexes."xsd:string |
| http://purl.uniprot.org/citations/17363702 | http://purl.uniprot.org/core/volume | "100"xsd:string |
| http://purl.uniprot.org/citations/17363702 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/17363702 |
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