2000
The Dopamine/D1 Receptor Mediates the Phosphorylation and Inactivation of the Protein Tyrosine Phosphatase STEP via a PKA-Dependent Pathway
Paul S, Snyder G, Yokakura H, Picciotto M, Nairn A, Lombroso P. The Dopamine/D1 Receptor Mediates the Phosphorylation and Inactivation of the Protein Tyrosine Phosphatase STEP via a PKA-Dependent Pathway. Journal Of Neuroscience 2000, 20: 5630-5638. PMID: 10908600, PMCID: PMC6772528, DOI: 10.1523/jneurosci.20-15-05630.2000.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAnimalsCatalytic DomainCorpus StriatumCyclic AMP-Dependent Protein KinasesEnzyme ActivationIn Vitro TechniquesMaleMolecular Sequence DataNeuronsPhosphoproteinsPhosphorus RadioisotopesPhosphorylationProtein Tyrosine PhosphatasesProtein Tyrosine Phosphatases, Non-ReceptorRatsRats, Sprague-DawleyReceptors, Dopamine D1Signal TransductionConceptsProtein tyrosine phosphatase familyCAMP-dependent protein kinaseTryptic phosphopeptide mappingPotential phosphorylation sitesUnique N-terminalProtein-protein interactionsMembrane-associated proteinsRole of phosphorylationTyrosine phosphatase familyAmino acid sequenceSite-directed mutagenesisAmino acid sequencingPKA-dependent pathwayTyrosine phosphatase STEPPhosphatase familyPhosphopeptide mappingPhosphorylation sitesAlternative splicingSubcellular compartmentsProtein kinaseTerminal domainEquivalent residuesCytosolic proteinsSpecific residuesAcid sequence
1999
Phylogenetically conserved CK‐II phosphorylation site of the murine homeodomain protein Hoxb‐6
Fienberg A, Nordstedt C, Belting H, Czernik A, Nairn A, Gandy S, Greengard P, Ruddle F. Phylogenetically conserved CK‐II phosphorylation site of the murine homeodomain protein Hoxb‐6. Journal Of Experimental Zoology 1999, 285: 76-84. PMID: 10327653, DOI: 10.1002/(sici)1097-010x(19990415)285:1<76::aid-jez9>3.0.co;2-k.Peer-Reviewed Original ResearchConceptsTwo-dimensional tryptic phosphopeptide mappingTryptic phosphopeptide mappingHoxb-6Casein kinase IIHomeodomain proteinsPhosphopeptide mappingPhosphorylation sitesHoxc-8Protein kinaseSf9 cellsCasein kinase II phosphorylation sitesKinase IICK-II phosphorylation sitesCAMP-dependent protein kinaseSignal transduction mechanismsBaculovirus expression systemProtein functionPhosphorylation stateMouse embryonic spinal cordExpression systemSerine 214Embryonic spinal cordTransduction mechanismsKinaseProteinInhibition of the Ca2+/Calmodulin-dependent Protein Kinase I Cascade by cAMP-dependent Protein Kinase*
Matsushita M, Nairn A. Inhibition of the Ca2+/Calmodulin-dependent Protein Kinase I Cascade by cAMP-dependent Protein Kinase*. Journal Of Biological Chemistry 1999, 274: 10086-10093. PMID: 10187789, DOI: 10.1074/jbc.274.15.10086.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCalcium-Calmodulin-Dependent Protein Kinase KinaseCalcium-Calmodulin-Dependent Protein Kinase Type 1Calcium-Calmodulin-Dependent Protein Kinase Type 4Calcium-Calmodulin-Dependent Protein KinasesCyclic AMP-Dependent Protein KinasesFeedbackHippocampusPC12 CellsPeptide MappingPhosphorylationProtein Serine-Threonine KinasesRatsSubstrate SpecificityConceptsActivation of PKACAMP-dependent protein kinaseDependent protein kinase IProtein kinaseProtein kinase IThreonine 108Kinase ITwo-dimensional phosphopeptide mappingDependent signal transduction pathwaysInhibition of CaMKKSignal transduction pathwaysIntact PC12 cellsRegulatory phosphorylationPhosphopeptide mappingTransduction pathwaysCaMKI activityCaMKKIntact cellsPhosphorylationPC12 cellsKinaseNegative feedback mechanismEnzyme cascadeEnzyme activityRapid inhibitionArginine vasopressin stimulates phosphorylation of aquaporin-2 in rat renal tissue
Nishimoto G, Zelenina M, Li D, Yasui M, Aperia A, Nielsen S, Nairn A. Arginine vasopressin stimulates phosphorylation of aquaporin-2 in rat renal tissue. American Journal Of Physiology 1999, 276: f254-f259. PMID: 9950956, DOI: 10.1152/ajprenal.1999.276.2.f254.Peer-Reviewed Original ResearchConceptsPhosphorylation of AQP2Protein kinase AAquaporin-2Two-dimensional phosphopeptide mappingCAMP-dependent protein kinase AConsensus phosphorylation sitesActivation of PKAPhosphopeptide mappingPhosphorylation sitesMaximal phosphorylationAQP2 phosphorylationKinase APhosphorylationSer256Immunoblot analysis
1993
Purification and characterization of calmodulin-dependent protein kinase III from rabbit reticulocytes and rat pancreas
Mitsui K, Brady M, Palfrey H, Nairn A. Purification and characterization of calmodulin-dependent protein kinase III from rabbit reticulocytes and rat pancreas. Journal Of Biological Chemistry 1993, 268: 13422-13433. PMID: 8514778, DOI: 10.1016/s0021-9258(19)38667-3.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsCalcium-Calmodulin-Dependent Protein KinasesCalmodulinCattleChromatography, GelElectrophoresis, Polyacrylamide GelElongation Factor 2 KinaseHeat-Shock ProteinsMolecular Sequence DataPancreasPeptide Elongation Factor 2Peptide Elongation FactorsPeptide MappingPhosphoproteinsPhosphorylationProtein KinasesRabbitsRatsReticulocytesSubstrate SpecificityConceptsEukaryotic elongation factor 2CaM kinase IIICalmodulin-dependent protein kinase IIIProtein kinase IIIKinase IIIProtein kinaseRabbit reticulocytesCAMP-dependent protein kinaseYeast EF-2Heat shock protein Hsp90Novel protein kinaseElongation factor 2Amino acid sequencingPhosphopeptide mappingSodium dodecyl sulfate-polyacrylamide gel electrophoresisDodecyl sulfate-polyacrylamide gel electrophoresisProtein Hsp90Catalytic subunitSulfate-polyacrylamide gel electrophoresisSeryl residuesMajor polypeptidesSubstrate ATPHsp90Factor 2Gel electrophoresis
1992
Characterization of the cystic fibrosis transmembrane conductance regulator in a colonocyte cell line.
Cohn J, Nairn A, Marino C, Melhus O, Kole J. Characterization of the cystic fibrosis transmembrane conductance regulator in a colonocyte cell line. Proceedings Of The National Academy Of Sciences Of The United States Of America 1992, 89: 2340-2344. PMID: 1372442, PMCID: PMC48653, DOI: 10.1073/pnas.89.6.2340.Peer-Reviewed Original ResearchConceptsCystic fibrosis transmembrane conductance regulatorFibrosis transmembrane conductance regulatorTransmembrane conductance regulatorConductance regulatorTwo-dimensional phosphopeptide mappingT84 cellsProtein kinase ACell linesProtein kinase CSDS/PAGEPhosphopeptide mappingPhosphorylation sitesProminent substrateCFTR peptidesEquivalent proteinsKinase ASame proteinKinase CTerminal sequenceCell lysatesN-glycanaseProteinAnti-peptide antibodiesImmunoblot signalsCFTR immunoreactivity
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