1997
Regulation of rat Na+-K+-ATPase activity by PKC is modulated by state of phosphorylation of Ser-943 by PKA
Cheng X, Höög J, Nairn A, Greengard P, Aperia A. Regulation of rat Na+-K+-ATPase activity by PKC is modulated by state of phosphorylation of Ser-943 by PKA. American Journal Of Physiology 1997, 273: c1981-c1986. PMID: 9435504, DOI: 10.1152/ajpcell.1997.273.6.c1981.Peer-Reviewed Original ResearchMeSH KeywordsAlanineAmino Acid SubstitutionAnimalsColforsinCOS CellsCyclic AMPCyclic AMP-Dependent Protein KinasesCytosolDichlororibofuranosylbenzimidazoleEnzyme ActivationHomeostasisIsoenzymesKineticsMutagenesis, Site-DirectedPhorbol 12,13-DibutyratePhosphorylationProtein Kinase CRatsRecombinant ProteinsSerineSodium-Potassium-Exchanging ATPaseThionucleotidesTransfectionConceptsProtein kinase AProtein kinase CATPase alpha 1State of phosphorylationEffect of PKCWild-type enzymeSpecific PKA activatorActivity of PKCEnzyme activityAlpha 1Direct phosphorylationCOS cellsATPase alphaKinase ASer-23Kinase CPKA activatorPhosphorylationPKA systemPhorbol esterATPase activityMutantsEffect of PDBuCellsInhibitionMutation of the Protein Kinase C Phosphorylation Site on Rat α1 Na+,K+-ATPase Alters Regulation of Intracellular Na+ and pH and Influences Cell Shape and Adhesiveness*
Belusa R, Wang Z, Matsubara T, Sahlgren B, Dulubova I, Nairn A, Ruoslahti E, Greengard P, Aperia A. Mutation of the Protein Kinase C Phosphorylation Site on Rat α1 Na+,K+-ATPase Alters Regulation of Intracellular Na+ and pH and Influences Cell Shape and Adhesiveness*. Journal Of Biological Chemistry 1997, 272: 20179-20184. PMID: 9242694, DOI: 10.1074/jbc.272.32.20179.Peer-Reviewed Original ResearchConceptsProtein kinase CProtein kinase APhosphorylation sitesProtein kinase C phosphorylation sitesKinase C phosphorylation sitesC phosphorylation sitesSites of phosphorylationATPase alpha1Influences cell shapePKC phosphorylation sitesEukaryotic cellsATP hydrolysisPKC phosphorylationRat α1COS cellsCell shapeKinase AWild typeSer-23Kinase CCell adhesionFunctional roleAlters regulationUntransfected cellsPhosphorylation
1994
Identification of the phosphorylation site for cAMP-dependent protein kinase on Na+,K(+)-ATPase and effects of site-directed mutagenesis.
Fisone G, Cheng S, Nairn A, Czernik A, Hemmings H, Höög J, Bertorello A, Kaiser R, Bergman T, Jörnvall H. Identification of the phosphorylation site for cAMP-dependent protein kinase on Na+,K(+)-ATPase and effects of site-directed mutagenesis. Journal Of Biological Chemistry 1994, 269: 9368-9373. PMID: 7510709, DOI: 10.1016/s0021-9258(17)37117-x.Peer-Reviewed Original ResearchMeSH Keywords1-Methyl-3-isobutylxanthineAmino Acid SequenceAnimalsBase SequenceColforsinCyclic AMP-Dependent Protein KinasesDNA PrimersKineticsMolecular Sequence DataMutagenesis, Site-DirectedPeptide MappingPeptidesPhosphoserineRatsRecombinant ProteinsSodium-Potassium-Exchanging ATPaseStructure-Activity RelationshipConceptsCAMP-dependent protein kinasePhosphorylation sitesProtein kinaseSignal transduction pathwaysWild-type enzymeSite-directed mutagenesisATPase alpha subunitAlpha 1 isoformCatalytic subunitTransduction pathwaysDependent phosphorylationSeryl residuesCOS cellsAlpha subunitIntact cellsATPaseKinasePhosphorylationEnzymeSubunitsCellsExperimental approachMutagenesisCDNAIsoforms