2001
Protein phosphatase 1 regulation by inhibitors and targeting subunits
Watanabe T, Huang H, Horiuchi A, da Cruze Silva E, Hsieh-Wilson L, Allen P, Shenolikar S, Greengard P, Nairn A. Protein phosphatase 1 regulation by inhibitors and targeting subunits. Proceedings Of The National Academy Of Sciences Of The United States Of America 2001, 98: 3080-3085. PMID: 11248035, PMCID: PMC30610, DOI: 10.1073/pnas.051003898.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsCell LineChromosomal Proteins, Non-HistoneDNA-Binding ProteinsDopamine and cAMP-Regulated Phosphoprotein 32Enzyme InhibitorsGene ExpressionHistone ChaperonesMicrofilament ProteinsMolecular Sequence DataMyelin Basic ProteinNerve Tissue ProteinsPhosphoprotein PhosphatasesPhosphoproteinsProtein Phosphatase 1ProteinsRabbitsRecombinant Fusion ProteinsSpodopteraSubstrate SpecificityTranscription FactorsConceptsProtein phosphatase 1Native protein phosphatase-1PP1 nuclear targeting subunitPhosphotyrosine-containing substratesInhibitor 2Protein phosphatase 1 regulationRecombinant protein phosphatase 1Sf9 insect cellsC-terminal sequencesLoss of interactionTargeting subunitPP1/Phosphatase 1Insect cellsResidues 274Inhibitor proteinRecombinant proteinsProtein inhibitorSubunitsEscherichia coliY272Corresponding regionPhosphorylase a.MutationsRegulation
2000
Regulation 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 receptorsActivationVivo
1998
Isolation and Characterization of PNUTS, a Putative Protein Phosphatase 1 Nuclear Targeting Subunit*
Allen P, Kwon Y, Nairn A, Greengard P. Isolation and Characterization of PNUTS, a Putative Protein Phosphatase 1 Nuclear Targeting Subunit*. Journal Of Biological Chemistry 1998, 273: 4089-4095. PMID: 9461602, DOI: 10.1074/jbc.273.7.4089.Peer-Reviewed Original ResearchConceptsPhosphatase 1 nuclear targeting subunitProtein phosphatase 1Targeting subunitPP1 catalytic activityMammalian cell lysatesTwo-hybrid assayPP1 functionsNuclear functionsNuclear compartmentalizationNovel proteinPhosphatase 1Subcellular localizationCell physiologyCell lysatesCell nucleiSubunitsExogenous substratesInitial characterizationProteinStable complexesPotent modulationChromatinCloningMitosisCompartmentalization
1997
Phosphorylation of Connexin43 and the Regulation of Neonatal Rat Cardiac Myocyte Gap Junctions
Sáez J, Nairn A, Czernik A, Fishman G, Spray D, Hertzberg E. Phosphorylation of Connexin43 and the Regulation of Neonatal Rat Cardiac Myocyte Gap Junctions. Journal Of Molecular And Cellular Cardiology 1997, 29: 2131-2145. PMID: 9281445, DOI: 10.1006/jmcc.1997.0447.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAnimals, NewbornCalcium-Calmodulin-Dependent Protein KinasesCDC2 Protein KinaseCells, CulturedConnexin 43DNA, ComplementaryElectrophoresis, Gel, Two-DimensionalEnzyme InhibitorsGap JunctionsMyocardiumPatch-Clamp TechniquesPhosphorylationProtein Processing, Post-TranslationalRatsRecombinant Fusion ProteinsStaurosporineTetradecanoylphorbol AcetateConceptsProtein kinase CTwo-dimensional tryptic phosphopeptide mapsTryptic phosphopeptide mapsState of phosphorylationMyocyte gap junctionsProtein kinase inhibitorsGap junctionsMajor gap junction proteinPhosphorylation of connexin43Gap junction proteinPhosphopeptide mapsTryptic phosphopeptidesPKC-dependent mechanismFunctional couplingPhosphorylated formKinase CPhosphorylationNeonatal rat cardiocytesCx43 phosphorylationStaurosporineCellular distributionImmunoblot analysisRat cardiocytesJunction proteinsCx43
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
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-transferase