2018
Striatal Signaling Regulated by the H3R Histamine Receptor in a Mouse Model of tic Pathophysiology
Rapanelli M, Frick L, Jindachomthong K, Xu J, Ohtsu H, Nairn A, Pittenger C. Striatal Signaling Regulated by the H3R Histamine Receptor in a Mouse Model of tic Pathophysiology. Neuroscience 2018, 392: 172-179. PMID: 30278251, PMCID: PMC6204318, DOI: 10.1016/j.neuroscience.2018.09.035.Peer-Reviewed Original ResearchConceptsHDC-KO miceMitogen-activated protein kinaseHistamine receptorsWT animalsDorsal striatumH3R activationTic-like movementsStriatonigral medium spiny neuronsAkt phosphorylationMedium spiny neuronsWild-type miceRare genetic causeHistamine dysregulationAgonist treatmentKO miceSpiny neuronsTic disordersTic pathophysiologyStriatal signalingMouse modelNeuropsychiatric diseasesKO modelRepetitive movementsStriatumMiceStriatin-1 is a B subunit of protein phosphatase PP2A that regulates dendritic arborization and spine development in striatal neurons
Li D, Musante V, Zhou W, Picciotto MR, Nairn AC. Striatin-1 is a B subunit of protein phosphatase PP2A that regulates dendritic arborization and spine development in striatal neurons. Journal Of Biological Chemistry 2018, 293: 11179-11194. PMID: 29802198, PMCID: PMC6052221, DOI: 10.1074/jbc.ra117.001519.Peer-Reviewed Original ResearchConceptsSerine/threonine phosphatase PP2AStriatin-interacting phosphataseRNA knockdown approachB subunitSTRIPAK complexPhosphatase PP2AProtein phosphataseMultiprotein complexesKnockdown approachStriatin familyMutant constructsStriatal neuronal culturesPP2ANeuronal developmentPrimary striatal neuronal culturesDendritic phenotypeKnockdown modelSynapse formationSubunitsSpine developmentSelective roleReduced expressionNeuron maturationNeuronal culturesStriatal neurons
2017
ARPP-16 Is a Striatal-Enriched Inhibitor of Protein Phosphatase 2A Regulated by Microtubule-Associated Serine/Threonine Kinase 3 (Mast 3 Kinase)
Andrade EC, Musante V, Horiuchi A, Matsuzaki H, Brody AH, Wu T, Greengard P, Taylor JR, Nairn AC. ARPP-16 Is a Striatal-Enriched Inhibitor of Protein Phosphatase 2A Regulated by Microtubule-Associated Serine/Threonine Kinase 3 (Mast 3 Kinase). Journal Of Neuroscience 2017, 37: 2709-2722. PMID: 28167675, PMCID: PMC5354324, DOI: 10.1523/jneurosci.4559-15.2017.Peer-Reviewed Original ResearchConceptsSerine/threonine protein phosphataseSerine/threonine kinase 3Threonine protein phosphataseARPP-16Protein phosphataseKinase 3Protein phosphatase 2AProtein kinase A (PKA) signalingSmall acid-soluble proteinsKinase A SignalingAcid-soluble proteinsActivation of PKAPP2A substratesPhosphatase 2AARPP-16/19Heterotrimeric formMarked dephosphorylationSignal transductionSelective inhibitorPP2AA SignalingUnknown functionStriatal medium spiny neuronsMedium spiny neuronsSer46
2003
Adenylyl cyclase-dependent form of chemical long-term potentiation triggers translational regulation at the elongation step
Chotiner J, Khorasani H, Nairn A, O’Dell T, Watson J. Adenylyl cyclase-dependent form of chemical long-term potentiation triggers translational regulation at the elongation step. Neuroscience 2003, 116: 743-752. PMID: 12573716, DOI: 10.1016/s0306-4522(02)00797-2.Peer-Reviewed Original ResearchConceptsEukaryotic elongation factor 2Elongation factor 2Elongation stepProtein synthesisTotal protein synthesisChemical long-term potentiationMessenger RNALong-term potentiationN-methyl-D-aspartate (NMDA) receptor-dependent formInhibition of translationFactor 2Long-term potentiation inductionTranslational regulationProtein ArcAdenylyl cyclase signalingAdenylyl cyclase activationSynaptic activityCyclase signalingN-methyl-D-aspartate (NMDA) receptor activationPersistent maintenanceReceptor-dependent formHippocampal long-term potentiationPhosphorylationRegulationRNA
2001
Regulation of cyclin-dependent kinase 5 and casein kinase 1 by metabotropic glutamate receptors
Liu F, Ma X, Ule J, Bibb J, Nishi A, DeMaggio A, Yan Z, Nairn A, Greengard P. Regulation of cyclin-dependent kinase 5 and casein kinase 1 by metabotropic glutamate receptors. Proceedings Of The National Academy Of Sciences Of The United States Of America 2001, 98: 11062-11068. PMID: 11572969, PMCID: PMC58683, DOI: 10.1073/pnas.191353898.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCalcium ChannelsCasein KinasesCyclin-Dependent Kinase 5Cyclin-Dependent KinasesDopamine and cAMP-Regulated Phosphoprotein 32Enzyme InhibitorsIn Vitro TechniquesKineticsMaleMembrane PotentialsMethoxyhydroxyphenylglycolMiceMice, Inbred C57BLNeostriatumNerve Tissue ProteinsNeuronsPatch-Clamp TechniquesPhosphoproteinsPhosphorylationPhosphoserinePhosphothreonineProtein KinasesReceptors, Metabotropic GlutamateConceptsCasein kinase 1Cyclin-dependent kinase 5Ser-137Thr-75CK1 activityKinase 1Kinase 5DARPP-32Regulation of Cdk5Neuronal protein kinaseActivation of Cdk5Cellular functionsProtein kinaseDNA repairEnhanced phosphorylationFirst messengersCdk5 activitySpecific inhibitorCdk5Effects of DHPGMetabotropic glutamate receptorsNeurite outgrowthIC261Glutamate receptorsDHPG-induced increaseTARPP, 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 GlandPhosphorylation 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
Amplification of dopaminergic signaling by a positive feedback loop
Nishi A, Bibb J, Snyder G, Higashi H, Nairn A, Greengard P. Amplification of dopaminergic signaling by a positive feedback loop. Proceedings Of The National Academy Of Sciences Of The United States Of America 2000, 97: 12840-12845. PMID: 11050161, PMCID: PMC18851, DOI: 10.1073/pnas.220410397.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCalcineurinCocaineCyclic AMP-Dependent Protein KinasesCyclin-Dependent Kinase 5Cyclin-Dependent KinasesDopamineDopamine and cAMP-Regulated Phosphoprotein 32FeedbackIn Vitro TechniquesMiceMice, Inbred C57BLNeostriatumNerve Tissue ProteinsPhosphoprotein PhosphatasesPhosphoproteinsPhosphorylationProtein Phosphatase 2Receptors, Dopamine D1Receptors, Dopamine D2Signal TransductionConceptsState of phosphorylationProtein kinaseThr-75Protein phosphatase 2A activityCAMP-dependent protein kinasePhosphatase 2A activityCyclin-dependent kinase 5DARPP-32Dopamine D1 receptor-mediated activationDopamine D2 receptor stimulationStriatal DARPP-32Receptor-mediated activationD2 receptor stimulationAction of dopamineEffects of dopaminePositive feedback loopPKA signalingKinase 5Inhibitory constraintPhosphorylationAcute cocaineWhole animalNeostriatal slicesReceptor stimulationDopaminergic signalingDrugs of abuse modulate the phosphorylation of ARPP-21, a cyclic AMP-regulated phosphoprotein enriched in the basal ganglia
Caporaso G, Bibb J, Snyder G, Valle C, Rakhilin S, Fienberg A, Hemmings H, Nairn A, Greengard P. Drugs of abuse modulate the phosphorylation of ARPP-21, a cyclic AMP-regulated phosphoprotein enriched in the basal ganglia. Neuropharmacology 2000, 39: 1637-1644. PMID: 10854908, DOI: 10.1016/s0028-3908(99)00230-0.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAntibodies, MonoclonalBasal GangliaCattleCocaineCorpus StriatumCyclosporineDopamine and cAMP-Regulated Phosphoprotein 32Dopamine Uptake InhibitorsEnzyme InhibitorsIllicit DrugsMarine ToxinsMethamphetamineMiceMice, Inbred C57BLMice, TransgenicNerve Tissue ProteinsOkadaic AcidOxazolesPhosphoproteinsPhosphorylationRatsRegulation of Phosphorylation of the GluR1 AMPA Receptor in the Neostriatum by Dopamine and Psychostimulants In Vivo
Snyder G, Allen P, Fienberg A, Valle C, Huganir R, Nairn A, Greengard P. Regulation of Phosphorylation of the GluR1 AMPA Receptor in the Neostriatum by Dopamine and Psychostimulants In Vivo. Journal Of Neuroscience 2000, 20: 4480-4488. PMID: 10844017, PMCID: PMC6772453, DOI: 10.1523/jneurosci.20-12-04480.2000.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBenzazepinesCentral Nervous System StimulantsDopamineDopamine and cAMP-Regulated Phosphoprotein 32In Vitro TechniquesMaleMethamphetamineMiceMice, Inbred C57BLMice, KnockoutMicrowavesNeostriatumNerve Tissue ProteinsOkadaic AcidPhosphoprotein PhosphatasesPhosphoproteinsPhosphorylationProtein Phosphatase 1Protein Phosphatase 2Receptors, AMPAReceptors, Dopamine D1Receptors, Dopamine D2Recombinant Fusion ProteinsSerineConceptsCAMP-dependent protein kinaseProtein phosphatase 2A.AMPA-type glutamate receptorsCalmodulin-dependent kinase IICalcium/calmodulin-dependent kinase IIRegulation of phosphorylationProtein kinase CPhosphatase 2A.Protein kinaseKinase IIPhosphorylation of GluR1Kinase CGluR1 AMPA receptorsPhosphorylationCellular effectorsGlutamate receptorsDARPP-32Physiological activityAMPA receptorsPsychostimulant cocaineChannel conductanceReceptorsD1-type dopamine receptorsActivationVivoSevere deficiencies in dopamine signaling in presymptomatic Huntington's disease mice
Bibb J, Yan Z, Svenningsson P, Snyder G, Pieribone V, Horiuchi A, Nairn A, Messer A, Greengard P. Severe deficiencies in dopamine signaling in presymptomatic Huntington's disease mice. Proceedings Of The National Academy Of Sciences Of The United States Of America 2000, 97: 6809-6814. PMID: 10829080, PMCID: PMC18747, DOI: 10.1073/pnas.120166397.Peer-Reviewed Original ResearchConceptsMedium spiny neuronsDisease miceSpiny neuronsStriatal medium spiny neuronsHuntington's diseaseSevere deficiencyHuntington's disease miceHD model miceModel miceDopaminergic neurotransmissionHD miceSelective neurodegenerationHD pathologyMiceDARPP-32DopamineHuman huntingtinBehavioral phenotypesDiseaseNeuronsIon channelsTotal levelsDisease-causing formHuntingtinDeficiency
1999
Requirement for DARPP‐32 in mediating effect of dopamine D2 receptor activation
Nishi A, Snyder G, Fienberg A, Fisone G, Aperia A, Nairn A, Greengard P. Requirement for DARPP‐32 in mediating effect of dopamine D2 receptor activation. European Journal Of Neuroscience 1999, 11: 2589-2592. PMID: 10383649, DOI: 10.1046/j.1460-9568.1999.00724.x.Peer-Reviewed Original ResearchConceptsDopamine D2 agonistD1 agonistDopamine D1 agonistDARPP-32D2 agonistDopamine D2 receptor activationDopamine D2 receptor agonistD2 receptor activationD2 receptor agonistBiological effectsReceptor agonistD1 receptorsD2 receptorsMouse neostriatumProtein phosphatase-1 inhibitorReceptor activationAgonistsPhosphatase-1 inhibitorDopamine signalingObligatory roleRole 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
1996
Developmental expression of MARCKS and protein kinase C in mice in relation to the exencephaly resulting from MARCKS deficiency
Blackshear P, Lai W, Tuttle J, Stumpo D, Kennington E, Nairn A, Sulik K. Developmental expression of MARCKS and protein kinase C in mice in relation to the exencephaly resulting from MARCKS deficiency. Brain Research 1996, 96: 62-75. PMID: 8922669, DOI: 10.1016/0165-3806(96)00097-1.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBeta-GalactosidaseEmbryonic and Fetal DevelopmentGene Expression Regulation, DevelopmentalGene Expression Regulation, EnzymologicImmunohistochemistryIntracellular Signaling Peptides and ProteinsIsoenzymesMembrane ProteinsMiceMice, Inbred C57BLMice, TransgenicMyristoylated Alanine-Rich C Kinase SubstrateNerve Tissue ProteinsNeural Tube DefectsPhosphorylationProtein Kinase CProteinsRecombinant Fusion ProteinsConceptsProtein kinase CNeural tube closureKinase CPlasma membraneTube closureNeural tubeCranial neural tube closureMajor cellular substrateEmbryonic day 8.5MARCKS deficiencySpecific cell typesE8.5 embryosCranial neural tubeMouse geneFunctional defectsMARCKS proteinPerinatal lethalityMARCKSCellular substratesCranial neurulationMARCKS expressionUnderlying mesenchymeDevelopmental expressionPKC-alphaDay 8.5