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 synthesisSubunitsMolecular identification of human G-substrate, a possible downstream component of the cGMP-dependent protein kinase cascade in cerebellar Purkinje cells
Endo S, Suzuki M, Sumi M, Nairn A, Morita R, Yamakawa K, Greengard P, Ito M. Molecular identification of human G-substrate, a possible downstream component of the cGMP-dependent protein kinase cascade in cerebellar Purkinje cells. Proceedings Of The National Academy Of Sciences Of The United States Of America 1999, 96: 2467-2472. PMID: 10051666, PMCID: PMC26808, DOI: 10.1073/pnas.96.5.2467.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBase SequenceBrainCerebellumCloning, MolecularCyclic GMP-Dependent Protein KinasesDatabases as TopicExpressed Sequence TagsHumansMolecular Sequence DataNerve Tissue ProteinsPurkinje CellsRabbitsRecombinant ProteinsRNA, MessengerSequence AlignmentSequence Homology, Amino AcidTranscription, GeneticConceptsAmino acid sequenceProtein phosphatase 1G-substrateAcid sequencePhosphatase 1Deduced amino acid sequenceRadiation hybrid panel analysisProtein phosphatase 2APutative phosphorylation sitesCGMP-dependent protein kinaseProtein kinase cascadeProtein phosphatase inhibitorSequence tag databaseSites of phosphorylationVitro translation productsHuman brain libraryCGMP-dependent proteinAcid-soluble proteinsApparent molecular massSDS/PAGEPhosphatase 2AThr-35Kinase cascadePhosphorylation sitesTag database
1997
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*
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
1991
[23] Production of phosphorylation state-specific antibodies
Jczernik A, Girault J, Nairn A, Chen J, Snyder G, Kebabian J, Greengard P. [23] Production of phosphorylation state-specific antibodies. Methods In Enzymology 1991, 201: 264-283. PMID: 1943769, DOI: 10.1016/0076-6879(91)01025-w.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsAntibodiesAntibodies, MonoclonalAntibody SpecificityCross ReactionsElectrophoresis, Polyacrylamide GelEnzyme-Linked Immunosorbent AssayGTP-Binding ProteinsImmunoblottingKineticsMolecular Sequence DataPeptidesPhosphopeptidesPhosphoproteinsPhosphorylationRabbitsRecombinant ProteinsSynapsinsConceptsPhosphorylation state-specific antibodiesState of phosphorylationSpecific substrate proteinsSites of phosphorylation
1990
Phosphorylation of connexin 32, a hepatocyte gap‐junction protein, by cAMP‐dependent protein kinase, protein kinase C and Ca2+/calmodulin‐dependent protein kinase II
SAEZ J, NAIRN A, CZERNIK A, SPRAY D, HERTZBERG E, GREENGARD P, BENNETT M. Phosphorylation of connexin 32, a hepatocyte gap‐junction protein, by cAMP‐dependent protein kinase, protein kinase C and Ca2+/calmodulin‐dependent protein kinase II. The FEBS Journal 1990, 192: 263-273. PMID: 2170122, DOI: 10.1111/j.1432-1033.1990.tb19223.x.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsCalcium-Calmodulin-Dependent Protein KinasesConnexinsElectrophoresis, Gel, Two-DimensionalElectrophoresis, Polyacrylamide GelFemaleLiverMembrane ProteinsMolecular Sequence DataPeptide FragmentsPeptidesPhosphopeptidesPhosphorylationProtein Kinase CProtein KinasesRatsRats, Inbred StrainsConceptsProtein kinase CCAMP-dependent protein kinaseDependent protein kinase IIGap junction proteinPhosphopeptide mappingProtein kinaseSeryl residuesProtein kinase IICAMP-PKKinase IIKinase CCell typesConnexin 32PK IIPhosphoamino acid analysisDifferent gap junction proteinsSites of phosphorylationPhosphorylated synthetic peptideCAMP-PK activityGap junctionsAmino acid sequencingActivation of PKCDifferent cell typesPhysiological substratesSynthetic peptides