1999
Mutation of Tyr307 and Leu309 in the Protein Phosphatase 2A Catalytic Subunit Favors Association with the α4 Subunit Which Promotes Dephosphorylation of Elongation Factor-2 †
Chung H, Nairn A, Murata K, Brautigan D. Mutation of Tyr307 and Leu309 in the Protein Phosphatase 2A Catalytic Subunit Favors Association with the α4 Subunit Which Promotes Dephosphorylation of Elongation Factor-2 †. Biochemistry 1999, 38: 10371-10376. PMID: 10441131, DOI: 10.1021/bi990902g.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAnion Exchange ResinsBacterial ProteinsCatalytic DomainChromatography, Ion ExchangeCOS CellsHemagglutininsLectinsLeucineMutagenesis, Site-DirectedOligopeptidesPeptide Elongation Factor 2Peptide Elongation FactorsPeptidesPhosphoprotein PhosphatasesPhosphoproteinsPhosphorylationPrecipitin TestsProtein Phosphatase 2Resins, SyntheticTransfectionTyrosineConceptsAlpha 4 proteinElongation factor 2AC dimerC subunitSpecific intracellular substratesProtein phosphatase 2ASites of phosphorylationAbc trimerCOS-7 cellsFactor 2B subunitC-terminal residuesTOR proteinsPhosphatase 2ANovel subunitCatalytic subunitTransient overexpressionSubstrate specificityCellular locationIntracellular substratesTransient expressionP70S6 kinaseSingle mutationProtein synthesisSubunits
1998
Regulation of Secretion of Alzheimer Amyloid Precursor Protein by the Mitogen‐Activated Protein Kinase Cascade
Desdouits‐Magnen J, Desdouits F, Takeda S, Syu L, Saltiel A, Buxbaum J, Czernik A, Nairn A, Greengard P. Regulation of Secretion of Alzheimer Amyloid Precursor Protein by the Mitogen‐Activated Protein Kinase Cascade. Journal Of Neurochemistry 1998, 70: 524-530. PMID: 9453546, DOI: 10.1046/j.1471-4159.1998.70020524.x.Peer-Reviewed Original ResearchMeSH KeywordsAmyloid beta-PeptidesAmyloid beta-Protein PrecursorAnimalsCalcium-Calmodulin-Dependent Protein KinasesCarbacholCHO CellsCOS CellsCricetinaeEnzyme ActivationEnzyme InhibitorsFlavonoidsHumansIndolesMaleimidesMitogen-Activated Protein Kinase KinasesMuscarinic AgonistsNerve Growth FactorsPC12 CellsPhorbol 12,13-DibutyrateProtein Kinase InhibitorsProtein KinasesRatsReceptor, Muscarinic M1Receptors, MuscarinicConceptsProtein kinase CAlzheimer amyloid precursor proteinKinase cascadeM1 muscarinic receptor stimulationMitogen-Activated Protein Kinase CascadeProtein kinase cascadeMAP kinase cascadeMAP kinase kinaseMAP kinase-independent pathwayMitogen-activated protein kinase kinase activationDominant negative mutantPrecursor proteinDistinct secretory pathwaysPKC-independent pathwayStimulation of PKCAmyloid precursor proteinKinase-independent pathwaySAPP secretionKinase kinaseSecretory pathwayNegative mutantMAP kinaseKinase activationRegulation of secretionPD 98059
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