2008
DARPP-32 Mediates the Actions of Multiple Drugs of Abuse
Svenningsson P, Nairn A, Greengard P. DARPP-32 Mediates the Actions of Multiple Drugs of Abuse. 2008, 3-16. DOI: 10.1007/978-0-387-76678-2_1.Peer-Reviewed Original ResearchPhosphorylation stateSerine/threonine protein phosphatasePP-1DARPP-32Threonine protein phosphataseState of phosphorylationProtein kinase A.Protein kinase AProtein phosphatasePhosphorylation sitesVirtue of regulationKinase AKey rolePhosphorylationThr34Potent inhibitorAdditional neurotransmittersCK2Ser97Behavioral responsesPhosphoproteinInhibitorsCK1Thr75Protein
2001
Opposing Changes in Phosphorylation of Specific Sites in Synapsin I During Ca2+-Dependent Glutamate Release in Isolated Nerve Terminals
Jovanovic J, Sihra T, Nairn A, Hemmings H, Greengard P, Czernik A. Opposing Changes in Phosphorylation of Specific Sites in Synapsin I During Ca2+-Dependent Glutamate Release in Isolated Nerve Terminals. Journal Of Neuroscience 2001, 21: 7944-7953. PMID: 11588168, PMCID: PMC6763853, DOI: 10.1523/jneurosci.21-20-07944.2001.Peer-Reviewed Original ResearchConceptsDependent dephosphorylationProtein phosphatase 2AMultiple protein kinasesPhosphorylation site 1Protein phosphatase 2BSynapsin IPhosphatase 2APhosphorylation sitesPhosphatase 2BSynapsin functionProtein kinaseDependent phosphorylationSynapsin I phosphorylationDephosphorylation processNeuronal phosphoproteinSynapsin I.Synaptic vesiclesCalcineurin activityPhosphorylationI phosphorylationDephosphorylationNeurotransmitter releaseSpecific sitesExcellent substrateSite 1Phosphorylation of Protein Phosphatase Inhibitor-1 by Cdk5*
Bibb J, Nishi A, O'Callaghan J, Ule J, Lan M, Snyder G, Horiuchi A, Saito T, Hisanaga S, Czernik A, Nairn A, Greengard P. Phosphorylation of Protein Phosphatase Inhibitor-1 by Cdk5*. Journal Of Biological Chemistry 2001, 276: 14490-14497. PMID: 11278334, DOI: 10.1074/jbc.m007197200.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBinding SitesBrainCalcineurinCarrier ProteinsCDC2 Protein KinaseCyclic AMPCyclic AMP-Dependent Protein KinasesCyclin-Dependent Kinase 5Cyclin-Dependent KinasesGlutamic AcidIntracellular Signaling Peptides and ProteinsKineticsMiceMice, Inbred C57BLMutagenesis, Site-DirectedN-MethylaspartatePhosphoprotein PhosphatasesPhosphorylationProlineProtein Phosphatase 1RabbitsRatsRecombinant ProteinsRNA-Binding ProteinsSerineTime FactorsConceptsProtein phosphatase inhibitor-1Protein phosphatase 1Phosphatase inhibitor-1Ser-67Protein kinasePhosphatase 1CAMP-dependent protein kinase resultsSelective protein kinase inhibitorsCAMP-dependent protein kinaseProtein phosphatase 2AProline-directed kinasesMitogen-activated protein kinaseInhibitor-1Protein kinase resultsSignal transduction eventsPhosphorylation state-specific antibodiesCAMP-dependent protein kinase activationState of phosphorylationProtein kinase inhibitorsProtein kinase activationPhosphatase 2AThr-35Protein phosphatasePhosphorylation sitesGlutamate-dependent regulation
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 mechanismsKinaseProteinMolecular 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 databaseArginine 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
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
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
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 immunoreactivityMechanism of desensitization of the epidermal growth factor receptor protein-tyrosine kinase.
Countaway J, Nairn A, Davis R. Mechanism of desensitization of the epidermal growth factor receptor protein-tyrosine kinase. Journal Of Biological Chemistry 1992, 267: 1129-1140. PMID: 1309762, DOI: 10.1016/s0021-9258(18)48406-2.Peer-Reviewed Original ResearchConceptsProtein tyrosine kinase activityKinase activityEGF receptorIntrinsic protein tyrosine kinase activityGrowth factor receptor protein tyrosine kinaseSrc homology 2 (SH2) regionsEpidermal growth factor receptor protein tyrosine kinaseEGF receptor protein tyrosine kinase activityReceptor protein tyrosine kinaseRegulatory phosphorylation sitesEGF-stimulated phosphorylationCalmodulin-dependent protein kinase IIProtein tyrosine kinasesEGF-stimulated endocytosisProtein kinase IICell surface receptorsEpidermal growth factor receptorPhosphorylation sitesBinding of EGFSignal transductionGrowth factor receptorCarboxyl terminusSer1046/7Kinase IIEGF treatment
1991
Identification and localization of a dogfish homolog of human cystic fibrosis transmembrane conductance regulator.
Marshall J, Martin K, Picciotto M, Hockfield S, Nairn A, Kaczmarek L. Identification and localization of a dogfish homolog of human cystic fibrosis transmembrane conductance regulator. Journal Of Biological Chemistry 1991, 266: 22749-22754. PMID: 1718999, DOI: 10.1016/s0021-9258(18)54631-7.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBase SequenceCell MembraneCloning, MolecularCystic FibrosisCystic Fibrosis Transmembrane Conductance RegulatorDNADogfishHumansImmunoenzyme TechniquesMembrane ProteinsMolecular Sequence DataMolecular WeightProtein KinasesRectumSebaceous GlandsSequence Homology, Nucleic AcidSubstrate SpecificityConceptsCystic fibrosis transmembrane conductance regulatorHuman cystic fibrosis transmembrane conductance regulatorFibrosis transmembrane conductance regulatorTransmembrane conductance regulatorDogfish proteinRectal glandConductance regulatorPutative substrate sitesCyclic AMP-dependent protein kinaseAMP-dependent protein kinaseMajor phosphorylation siteCyclic AMP-dependent protein phosphorylationApical plasma membraneAmino acid sequenceStudy of regulationPhosphorylation sitesProtein phosphorylationCDNA clonesProtein kinaseSimilar molecular massCFTR sequencePlasma membraneAcid sequenceImmunolocalization studiesMolecular massProtein kinase C substrate and inhibitor characteristics of peptides derived from the myristoylated alanine-rich C kinase substrate (MARCKS) protein phosphorylation site domain
Graff J, Rajan R, Randall R, Nairn A, Blackshear P. Protein kinase C substrate and inhibitor characteristics of peptides derived from the myristoylated alanine-rich C kinase substrate (MARCKS) protein phosphorylation site domain. Journal Of Biological Chemistry 1991, 266: 14390-14398. PMID: 1650359, DOI: 10.1016/s0021-9258(18)98697-7.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceCalcium-Calmodulin-Dependent Protein KinasesIntracellular Signaling Peptides and ProteinsMembrane ProteinsMolecular Sequence DataMyristoylated Alanine-Rich C Kinase SubstratePeptidesPhosphopeptidesPhosphorylationProtein Kinase CProtein KinasesProteinsSerineSubstrate SpecificityTrypsinConceptsProtein kinase CCGMP-dependent protein kinasePhosphorylation site domainCatalytic fragmentKinase CProtein kinaseSite domainProtein kinase C substrateProtein kinase C phosphorylationDependent protein kinase IAlanine-rich C kinase substrateKinase C phosphorylationC kinase substrateProtein kinase IProtein kinase IIHigh-affinity substrateKinase substratePhosphorylation sitesTryptic phosphopeptidesKinase IBasic regionMARCKS proteinProtein consistC phosphorylationKinase II
1989
Multisite phosphorylation of microtubule-associated protein 2 (MAP-2) in rat brain: Peptide mapping distinguishes between cyclic AMP-, calcium/calmodulin-, and calcium/phospholipid-regulated phosphorylation mechanisms
Walaas S, Nairn A. Multisite phosphorylation of microtubule-associated protein 2 (MAP-2) in rat brain: Peptide mapping distinguishes between cyclic AMP-, calcium/calmodulin-, and calcium/phospholipid-regulated phosphorylation mechanisms. Journal Of Molecular Neuroscience 1989, 1: 117-127. DOI: 10.1007/bf02918897.Peer-Reviewed Original ResearchCalcium/phospholipid-dependent protein kinasePhospholipid-dependent protein kinaseCalmodulin-dependent protein kinase IICalcium/calmodulin-dependent protein kinase IIProtein kinaseCalcium/calmodulinProtein kinase IIKinase IICyclic AMP-dependent protein kinaseAMP-dependent protein kinaseCommon phosphorylation sitesOnly serine residuesProtein 2Cyclic AMPMultisite phosphorylationThreonine residuesPhosphorylation sitesSerine residuesPhosphorylation systemPhosphorylation mechanismCytoskeletal proteinsMAP-2KinasePeptide mapsDistinct sitesIdentification of two protein kinases that phosphorylate the neural cell-adhesion molecule, N-CAM
Mackie K, Sorkin B, Nairn A, Greengard P, Edelman G, Cunningham B. Identification of two protein kinases that phosphorylate the neural cell-adhesion molecule, N-CAM. Journal Of Neuroscience 1989, 9: 1883-1896. PMID: 2542481, PMCID: PMC6569722, DOI: 10.1523/jneurosci.09-06-01883.1989.Peer-Reviewed Original ResearchConceptsProtein kinaseLarge polypeptidesCytoplasmic domainKinase ICell adhesion moleculeNeural cell adhesion moleculeThreonyl residuesCalmodulin-dependent protein kinase IN-CAMCalcium/calmodulin-dependent protein kinase ICyclic AMP-dependent protein kinaseCyclic GMP-dependent protein kinaseGlycogen synthase kinase-3AMP-dependent protein kinaseCommon phosphorylation sitesGMP-dependent protein kinaseCasein kinase IISynthase kinase-3Protein kinase IN-CAM polypeptidesChicken N-CAMProtein kinase CPrior phosphorylationPhosphorylation sitesAlternative splicingMultisite phosphorylation of microtubule-associated protein 2 (MAP-2) in rat brain: Peptide mapping distinguishes between cyclic AMP-, calcium/calmodulin-, and calcium/phospholipid-regulated phosphorylation mechanisms
Ivar Walaas S, Nairn A. Multisite phosphorylation of microtubule-associated protein 2 (MAP-2) in rat brain: Peptide mapping distinguishes between cyclic AMP-, calcium/calmodulin-, and calcium/phospholipid-regulated phosphorylation mechanisms. Journal Of Molecular Neuroscience 1989, 1: 117-127. PMID: 2561875, DOI: 10.1007/bf02896895.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAmino AcidsAnimalsBrainCalcium-Calmodulin-Dependent Protein KinasesElectrophoresis, Gel, Two-DimensionalElectrophoresis, Polyacrylamide GelMicrotubule-Associated ProteinsOrgan SpecificityPeptide MappingPhosphopeptidesPhosphorylationProtein Kinase CProtein KinasesRatsConceptsCalcium/phospholipid-dependent protein kinasePhospholipid-dependent protein kinaseCalmodulin-dependent protein kinase IICalcium/calmodulin-dependent protein kinase IIProtein kinaseCalcium/calmodulinProtein kinase IIKinase IICyclic AMP-dependent protein kinaseAMP-dependent protein kinaseCommon phosphorylation sitesOnly serine residuesProtein 2Cyclic AMPMultisite phosphorylationThreonine residuesPhosphorylation sitesSerine residuesPhosphorylation systemPhosphorylation mechanismCytoskeletal proteinsMAP-2KinasePeptide mapsDistinct sites