2016
Glutamate Counteracts Dopamine/PKA Signaling via Dephosphorylation of DARPP-32 Ser-97 and Alteration of Its Cytonuclear Distribution
Nishi A, Matamales M, Musante V, Valjent E, Kuroiwa M, Kitahara Y, Rebholz H, Greengard P, Girault JA, Nairn AC. Glutamate Counteracts Dopamine/PKA Signaling via Dephosphorylation of DARPP-32 Ser-97 and Alteration of Its Cytonuclear Distribution. Journal Of Biological Chemistry 2016, 292: 1462-1476. PMID: 27998980, PMCID: PMC5270488, DOI: 10.1074/jbc.m116.752402.Peer-Reviewed Original ResearchConceptsProtein phosphatase 1Ser-97PKA signalingDARPP-32Thr-34Activation of PP2A.Multiple cellular levelsProtein DARPP-32Phosphatase 1Heterotrimer complexPKA actionPhosphorylation stateNuclear localizationThr-75Phosphatase assaysDephosphorylationDARPP-32 phosphorylationCultured striatal neuronsSer-130Cellular levelSignalingPhosphorylationMajor siteStriatal neuronsGlutamate
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 1Angiotensin II regulates phosphorylation of translation elongation factor-2 in cardiac myocytes
Everett A, Stoops T, Nairn A, Brautigan D. Angiotensin II regulates phosphorylation of translation elongation factor-2 in cardiac myocytes. AJP Heart And Circulatory Physiology 2001, 281: h161-h167. PMID: 11406481, DOI: 10.1152/ajpheart.2001.281.1.h161.Peer-Reviewed Original ResearchMeSH KeywordsAngiotensin IIAnimalsCells, CulturedChromonesEnzyme InhibitorsMitogen-Activated Protein KinasesMorpholinesMyocardiumPeptide Elongation Factor 2Phosphoprotein PhosphatasesPhosphorylationProtein BiosynthesisProtein Phosphatase 2RatsRats, Sprague-DawleyReceptor, Angiotensin, Type 1Receptor, Angiotensin, Type 2Receptors, AngiotensinSignal TransductionSirolimusConceptsEukaryotic elongation factor 2Mitogen-activated protein kinaseElongation factor 2Protein phosphatase 2A inhibitor okadaic acidTranslation elongation factor 2Protein synthesisInhibitor okadaic acidFactor 2Rapamycin (mTOR) inhibitor rapamycinProtein translationDephosphorylated statePolypeptide elongationII-dependent increaseProtein kinaseEEF2 kinaseOkadaic acidDependent regulationInhibitor FK506MAPK activationPD 98059Cardiac myocytesDephosphorylationInhibitor rapamycinNeonatal cardiac myocytesRat neonatal cardiac myocytesElongation Factor-2 Phosphorylation and the Regulation of Protein Synthesis by Calcium
Nairn A, Matsushita M, Nastiuk K, Horiuchi A, Mitsui K, Shimizu Y, Palfrey H. Elongation Factor-2 Phosphorylation and the Regulation of Protein Synthesis by Calcium. Progress In Molecular And Subcellular Biology 2001, 27: 91-129. PMID: 11575162, DOI: 10.1007/978-3-662-09889-9_4.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsCalciumCalcium-Calmodulin-Dependent Protein KinasesCell CycleCell DivisionCyclic AMP-Dependent Protein KinasesCysteine EndopeptidasesElongation Factor 2 KinaseHumansMolecular Sequence DataMultienzyme ComplexesNeuronsPeptide Chain Elongation, TranslationalPeptide Elongation Factor 2PhosphorylationProteasome Endopeptidase ComplexProtein BiosynthesisSequence Homology, Amino AcidSignal TransductionUbiquitinConceptsProtein synthesisElongation factor 2 phosphorylationDephosphorylation of eEF2Eukaryotic protein synthesisAminoacyl-tRNA synthetasesFactor 2 phosphorylationElongation factor 2Ribosomal proteinsRegulated processInitiation factorsDependent kinasesKey proteinsRate of elongationPeptidyl-tRNAPhysiological roleKinasePhosphorylationFactor 2EEF2P siteThr56ProteinSynthetasesDephosphorylationRibosomes
2000
Prostaglandin E2 interaction with AVP: effects on AQP2 phosphorylation and distribution
Zelenina M, Christensen B, Palmér J, Nairn A, Nielsen S, Aperia A. Prostaglandin E2 interaction with AVP: effects on AQP2 phosphorylation and distribution. American Journal Of Physiology. Renal Physiology 2000, 278: f388-f394. PMID: 10710543, DOI: 10.1152/ajprenal.2000.278.3.f388.Peer-Reviewed Original ResearchConceptsTranslocation of AQP2AQP2 phosphorylationPlasma membraneAquaporin-2Subcellular distributionPlasma membrane-enriched fractionVesicle-enriched fractionsMembrane-enriched fractionDuct water permeabilityConsensus sitesIntracellular vesiclesPhosphorylationDifferential centrifugation techniqueAction of arginineRenal inner medullaE2 interactionRat renal inner medullaTranslocationInner medullaDose-dependent mannerWater channelsMembraneDephosphorylationTraffickingProtein
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 analysisRole of Calcineurin and Protein Phosphatase‐2A in the Regulation of DARPP‐32 Dephosphorylation in Neostriatal Neurons
Nishi A, Snyder G, Nairn A, Greengard P. Role of Calcineurin and Protein Phosphatase‐2A in the Regulation of DARPP‐32 Dephosphorylation in Neostriatal Neurons. Journal Of Neurochemistry 1999, 72: 2015-2021. PMID: 10217279, DOI: 10.1046/j.1471-4159.1999.0722015.x.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCalcineurinCalcineurin InhibitorsCyclosporineDopamine and cAMP-Regulated Phosphoprotein 32Drug CombinationsDrug SynergismEnzyme InhibitorsIn Vitro TechniquesMaleMarine ToxinsMiceMice, Inbred C57BLNeostriatumNerve Tissue ProteinsNeuronsOkadaic AcidOxazolesPhosphoprotein PhosphatasesPhosphoproteinsPhosphorylationProtein Phosphatase 1Protein Phosphatase 2ConceptsProtein phosphatase 1Protein phosphatase 2AOkadaic acidPhosphorylated DARPP-32DARPP-32 phosphorylationPhosphatase 2APP-2ADARPP-32Cyclic AMP-dependent protein kinaseAMP-dependent protein kinasePP-2A activityRole of calcineurinPhosphatase 1Calyculin AMouse neostriatal slicesProtein kinaseAction of cyclosporinDependent activationCalcineurinPresence of cyclosporinPhosphorylationDephosphorylationSynergistic increaseThr34Potent inhibitor
1994
Ca2+/Calmodulin-Dependent Protein Kinase V and I May Form a Family of Isoforms
Ito T, Yokokura H, Nairn A, Nimura Y, Hidaka H. Ca2+/Calmodulin-Dependent Protein Kinase V and I May Form a Family of Isoforms. Biochemical And Biophysical Research Communications 1994, 201: 1561-1566. PMID: 8024601, DOI: 10.1006/bbrc.1994.1882.Peer-Reviewed Original Research
1992
The role of protein phosphatases in synaptic transmission, plasticity and neuronal development
Nairn A, Shenolikar S. The role of protein phosphatases in synaptic transmission, plasticity and neuronal development. Current Opinion In Neurobiology 1992, 2: 296-301. PMID: 1322750, DOI: 10.1016/0959-4388(92)90118-5.Peer-Reviewed Original ResearchConceptsNeuronal developmentSerine/threonineRole of proteinsProtein phosphataseProtein dephosphorylationMolecular cloningTyrosine proteinIon channelsNervous systemPast year significant advancesNeuronal functionNeurotransmitter receptorsSpecific neuronsProteinSelective inhibitorEnzymeYears significant advancesSynaptic transmissionDephosphorylationCloningThreonineRolePhosphataseRegulationPlasticity
1991
Immunocytochemical localization of phosphatase inhibitor‐1 in rat brain
Gustafson E, Girault J, Hemmings H, Nairn A, Greengard P. Immunocytochemical localization of phosphatase inhibitor‐1 in rat brain. The Journal Of Comparative Neurology 1991, 310: 170-188. PMID: 1955581, DOI: 10.1002/cne.903100204.Peer-Reviewed Original ResearchConceptsPhosphatase inhibitor-1Inhibitor-1Intracellular signal transductionPhosphatase 1Protein phosphorylationSignal transductionWidespread roleNumerous immunoreactive cell bodiesSuprachiasmatic nucleusCyclic AMPImmunocytochemical localizationUse of immunocytochemistrySubstantial populationNeurotransmitter regulationDephosphorylationLocalizationNucleusTransductionImmunocytochemical studyCell bodiesPhosphorylationProteinNeuronsRegulationHigh levels