2001
TARPP, a novel protein that accompanies TCR gene rearrangement and thymocyte education
Kisielow J, Nairn A, Karjalainen K. TARPP, a novel protein that accompanies TCR gene rearrangement and thymocyte education. European Journal Of Immunology 2001, 31: 1141-1149. PMID: 11298339, DOI: 10.1002/1521-4141(200104)31:4<1141::aid-immu1141>3.0.co;2-r.Peer-Reviewed Original ResearchAgingAmino Acid SequenceAnimalsAntibodiesBase SequenceCD3 ComplexCell DifferentiationCell LineageCells, CulturedCloning, MolecularDown-RegulationFlow CytometryGene Expression ProfilingGene Expression Regulation, DevelopmentalGene Rearrangement, T-LymphocyteMiceMice, Inbred C57BLMolecular Sequence DataMolecular WeightPhosphoproteinsProtein Phosphatase 1Receptors, Antigen, T-CellRNA, MessengerSignal TransductionThymus GlandDecreased levels of ARPP-19 and PKA in brains of Down syndrome and Alzheimer’s disease
Kim S, Nairn A, Cairns N, Lubec G. Decreased levels of ARPP-19 and PKA in brains of Down syndrome and Alzheimer’s disease. Journal Of Neural Transmission. Supplementa 2001, 263-272. PMID: 11771749, DOI: 10.1007/978-3-7091-6262-0_21.Peer-Reviewed Original ResearchConceptsARPP-19Protein kinaseDifferential display polymerase chain reactionAlzheimer's diseaseDown syndromeCAMP-dependent protein kinaseTemporal cortexActivity of PKASignal transductionDownregulated sequenceBrain regionsNeurodegenerative disordersDiseaseImpaired mechanismsProtein levelsDecreased activityChain reactionFirst evidenceSignificant reductionSyndromeCortexDisordersTransductionHomologyKinase
2000
Severed Channels Probe Regulation of Gating of Cystic Fibrosis Transmembrane Conductance Regulator by Its Cytoplasmic Domains
Csanády L, Chan K, Seto-Young D, Kopsco D, Nairn A, Gadsby D. Severed Channels Probe Regulation of Gating of Cystic Fibrosis Transmembrane Conductance Regulator by Its Cytoplasmic Domains. The Journal Of General Physiology 2000, 116: 477-500. PMID: 10962022, PMCID: PMC2233695, DOI: 10.1085/jgp.116.3.477.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAdenylyl ImidodiphosphateAnimalsBase SequenceCyclic AMP-Dependent Protein KinasesCystic FibrosisCystic Fibrosis Transmembrane Conductance RegulatorDNA PrimersFemaleHumansIn Vitro TechniquesIon Channel GatingModels, BiologicalMutationOocytesPhosphorylationProtein Structure, TertiaryRecombinant ProteinsXenopusConceptsR domainCFTR channelsPhosphorylated R domainWild-type CFTR channelsCytoplasmic regulatory domainCystic fibrosis transmembrane conductance regulatorNucleotide Binding DomainFibrosis transmembrane conductance regulatorDetailed functional characteristicsWT channelsApparent ATP affinityTransmembrane conductance regulatorCFTR Cl- channelPresence of PKANonhydrolyzable ATP analogue AMPPNPATP analogue AMPPNPATP bindingRegulatory domainCytoplasmic domainWt-CFTRBinding domainsGating eventsConductance regulatorATP affinityFunctional interactionCellular Mechanisms Regulating Protein Phosphatase-1 A KEY FUNCTIONAL INTERACTION BETWEEN INHIBITOR-2 AND THE TYPE 1 PROTEIN PHOSPHATASE CATALYTIC SUBUNIT*
Frederick D, Huang H, Yang J, Helps N, Cohen P, Nairn A, DePaoli-Roach A, Tatchell K, Connor J, Shenolikar S. Cellular Mechanisms Regulating Protein Phosphatase-1 A KEY FUNCTIONAL INTERACTION BETWEEN INHIBITOR-2 AND THE TYPE 1 PROTEIN PHOSPHATASE CATALYTIC SUBUNIT*. Journal Of Biological Chemistry 2000, 275: 18670-18675. PMID: 10748125, DOI: 10.1074/jbc.m909312199.Peer-Reviewed Original ResearchConceptsPP1 catalytic subunitCatalytic subunitType 1 protein phosphatase catalytic subunitAmino acidsProtein phosphatase catalytic subunitN-terminusProtein serine/threonineN-terminal 35 amino acidsInhibitor 2Phosphatase catalytic subunitTwo-hybrid analysisNovel regulatory interactionsProtein phosphatase 1Serine/threoninePull-down assaysSite-directed mutagenesisN-terminal sequencePP1 mutantsKey functional interactionsPP1 inhibitorPP1 enzymesPP1 inhibitionPhosphatase 1Regulatory interactionsSaccharomyces cerevisiae
1999
Modulation of GT-1 DNA-binding activity by calcium-dependent phosphorylation
Maréchal E, Hiratsuka K, Delgado J, Nairn A, Qin J, Chait B, Chua N. Modulation of GT-1 DNA-binding activity by calcium-dependent phosphorylation. Plant Molecular Biology 1999, 40: 373-386. PMID: 10437822, DOI: 10.1023/a:1006131330930.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsArabidopsisBase SequenceBinding SitesCalciumCalcium-Calmodulin-Dependent Protein Kinase Type 2Calcium-Calmodulin-Dependent Protein KinasesDNA PrimersDNA-Binding ProteinsIn Vitro TechniquesMolecular Sequence DataNuclear ProteinsPhosphorylationPlants, ToxicRatsRecombinant ProteinsSequence Homology, Amino AcidSubstrate SpecificityTranscription FactorsConceptsDNA-binding activityCalcium-dependent phosphorylationGene expressionMolecular switchGT-1Analysis of mutantsDNA-binding proteinsLight-grown plantsPost-translational modificationsCalf intestine phosphataseCalcium/calmodulin kinasePhosphorylatable residuesCasein kinaseGene activationMass spectrometry analysisPromoter sequencesDNA bindingKinase activityBoxIICalmodulin kinasePhosphorylationHGT-1Novo synthesisDephosphorylationSpectrometry analysisMolecular 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
1995
The Regulatory Region of Calcium/Calmodulin-dependent Protein Kinase I Contains Closely Associated Autoinhibitory and Calmodulin-binding Domains (∗)
Yokokura H, Picciotto M, Nairn A, Hidaka H. The Regulatory Region of Calcium/Calmodulin-dependent Protein Kinase I Contains Closely Associated Autoinhibitory and Calmodulin-binding Domains (∗). Journal Of Biological Chemistry 1995, 270: 23851-23859. PMID: 7559563, DOI: 10.1074/jbc.270.40.23851.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBase SequenceBinding SitesCalcium-Calmodulin-Dependent Protein Kinase Type 1Calcium-Calmodulin-Dependent Protein KinasesCalmodulinDNA, ComplementaryEnzyme InhibitorsIn Vitro TechniquesMolecular Sequence DataMutagenesisMyosin-Light-Chain KinaseRatsRecombinant Fusion ProteinsSequence DeletionSequence Homology, Amino AcidStructure-Activity RelationshipConceptsCaM kinase IKinase IProtein kinase ITruncation mutantsCalmodulin-dependent protein kinase ICalcium/calmodulin-dependent protein kinase IDependent protein kinase IDependent protein kinaseSyntide-2Active kinaseAutoinhibitory domainDependent activityGlutathione S-transferaseProtein kinaseRegulatory regionsActive mutantMutantsFusion proteinPeptide substratesIntrasteric mechanismGlutathione-Sepharose 4B.COOH-terminalS-transferaseRapamycin inhibits ribosomal protein synthesis and induces G1 prolongation in mitogen-activated T lymphocytes.
Terada N, Takase K, Papst P, Nairn A, Gelfand E. Rapamycin inhibits ribosomal protein synthesis and induces G1 prolongation in mitogen-activated T lymphocytes. The Journal Of Immunology 1995, 155: 3418-26. PMID: 7561036, DOI: 10.4049/jimmunol.155.7.3418.Peer-Reviewed Original ResearchConceptsCell cycle progressionRibosomal protein mRNAsCycle progressionG2/M phaseRibosomal proteinsProtein synthesisProtein mRNAG1 prolongationCell cycleS phaseRibosomal protein mRNA translationRibosomal protein synthesisM phaseTotal cellular proteinEffect of rapamycinDNA synthesisNumber of ribosomesCell sizeCellular proteinsMRNA translationPhosphorylation of DARPP-32, a Dopamine- and cAMP-regulated Phosphoprotein, by Casein Kinase I in Vitro and in Vivo *
Desdouits F, Cohen D, Nairn A, Greengard P, Girault J. Phosphorylation of DARPP-32, a Dopamine- and cAMP-regulated Phosphoprotein, by Casein Kinase I in Vitro and in Vivo *. Journal Of Biological Chemistry 1995, 270: 8772-8778. PMID: 7721783, DOI: 10.1074/jbc.270.15.8772.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBase SequenceCasein KinasesCattleCorpus StriatumCyclic AMPDNA PrimersDopamineDopamine and cAMP-Regulated Phosphoprotein 32Electrophoresis, Polyacrylamide GelHumansMolecular Sequence DataMutagenesis, Site-DirectedNerve Tissue ProteinsNeuronsPeptide MappingPhosphoproteinsPhosphorylationProtein KinasesRabbitsRatsSubstantia NigraConceptsCasein kinase IProtein phosphatase 1Kinase ISer-137Phosphatase 1Ser-189DARPP-32CAMP-dependent protein kinasePhosphatase-1 inhibitorStoichiometry of phosphorylationSite-directed mutagenesisSpecific cell populationsProtein kinaseProtein sequencingSeryl residuesAcidic residuesThr-34PhosphorylationPhosphate/Presence of SDSChoroid plexus epithelial cellsResiduesCell populationsElectrophoretic mobilityEpithelial cells
1994
Rapamycin selectively inhibits translation of mRNAs encoding elongation factors and ribosomal proteins.
Terada N, Patel H, Takase K, Kohno K, Nairn A, Gelfand E. Rapamycin selectively inhibits translation of mRNAs encoding elongation factors and ribosomal proteins. Proceedings Of The National Academy Of Sciences Of The United States Of America 1994, 91: 11477-11481. PMID: 7972087, PMCID: PMC45254, DOI: 10.1073/pnas.91.24.11477.Peer-Reviewed Original ResearchConceptsRibosomal proteinsElongation factorProtein synthesisRibosomal protein mRNAsRibosomal protein synthesisTranslation of mRNAsP70 S6 kinaseRibosomal S6 proteinElongation factor 2Higher eukaryotesNonribosomal proteinsPolysomal associationRate of biosynthesisTranslational regulationMammalian cellsMRNA translationS6 kinaseAddition of rapamycinS6 proteinSubsequent phosphorylationEEF-2Translational levelImmunosuppressant rapamycinQuiescent cellsSelective proteinsIdentification 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
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 mass