2018
Striatin-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
1997
Characterization of novel calmodulin-binding peptides with distinct inhibitory effects on calmodulin-dependent enzymes
NEVALAINEN L, AOYAMA T, IKURA M, CRIVICI A, Hong Y, CHUA N, NAIRN A. Characterization of novel calmodulin-binding peptides with distinct inhibitory effects on calmodulin-dependent enzymes. Biochemical Journal 1997, 321: 107-115. PMID: 9003408, PMCID: PMC1218043, DOI: 10.1042/bj3210107.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCalcium-Calmodulin-Dependent Protein Kinase Type 2Calcium-Calmodulin-Dependent Protein KinasesCalmodulinCalmodulin-Binding ProteinsCattleCyclic Nucleotide Phosphodiesterases, Type 1Magnetic Resonance SpectroscopyMaleNeurosporaPeptide MappingPhosphoric Diester HydrolasesSpectrometry, FluorescenceTestis
1996
Amyloid β Peptide Formation in Cell-free Preparations REGULATION BY PROTEIN KINASE C, CALMODULIN, AND CALCINEURIN*
Desdouits F, Buxbaum J, Desdouits-Magnen J, Nairn A, Greengard P. Amyloid β Peptide Formation in Cell-free Preparations REGULATION BY PROTEIN KINASE C, CALMODULIN, AND CALCINEURIN*. Journal Of Biological Chemistry 1996, 271: 24670-24674. PMID: 8798734, DOI: 10.1074/jbc.271.40.24670.Peer-Reviewed Original ResearchMeSH KeywordsAmyloid beta-PeptidesCalcineurinCalmodulinCalmodulin-Binding ProteinsCell-Free SystemHumansPeptide FragmentsPhosphoprotein PhosphatasesPhosphorylationProtein Kinase CConceptsProtein kinase CAction of PKCCell-free systemIntact cellsKinase CProtein phosphatase calcineurinCell-permeant inhibitorStimulation of PKCSpecific peptide inhibitorPhosphatase calcineurinMolecular mechanismsCalcineurinPeptide inhibitorRegulationShort peptidesCalmodulinCellsBeta peptideInhibitorsPeptide formationPeptidesMajor constituentsPronounced inhibitionCyclosporin ASingle substrate
1995
A Role for Calcineurin (Protein Phosphatase-2B) in the Regulation of Glutamate Release
Sihra T, Nairn A, Kloppenburg P, Lin Z, Pouzat C. A Role for Calcineurin (Protein Phosphatase-2B) in the Regulation of Glutamate Release. Biochemical And Biophysical Research Communications 1995, 212: 609-616. PMID: 7542882, DOI: 10.1006/bbrc.1995.2013.Peer-Reviewed Original ResearchConceptsRelease of glutamateGlutamate releaseVoltage-dependent Ca channel activityVoltage-dependent Ca influxRat cerebral cortexCa-dependent componentCa channel activityCerebral cortexNerve terminalsCa influxInflux of CaCa entryActivation of calcineurinCa channelsCalcineurin activityGlutamateFK506CalcineurinRelease
1994
Correlation between protein kinase C binding proteins and substrates in REF52 cells.
Hyatt S, Liao L, Aderem A, Nairn A, Jaken S. Correlation between protein kinase C binding proteins and substrates in REF52 cells. Molecular Cancer Research 1994, 5: 495-502. PMID: 8049156.Peer-Reviewed Original ResearchMeSH KeywordsBlotting, WesternCalmodulin-Binding ProteinsCell LineCell Line, TransformedCell Transformation, NeoplasticDown-RegulationIntracellular Signaling Peptides and ProteinsIsoenzymesMembrane ProteinsMolecular WeightMyristoylated Alanine-Rich C Kinase SubstratePhosphatidylserinesPhosphorylationProtein BindingProtein DenaturationProtein Kinase CProtein Kinase C-alphaProteinsSolubilityConceptsProtein kinase CREF52 cellsPKC substrateKinase CBinding proteinProperties of PKCCalmodulin-Sepharose chromatographyBlot overlay assaysProteins/substratesMajor PKC substrateMajor binding proteinPhosphorylation assaysBlot overlayOverlay assaysTarget proteinsBasal phosphorylationProteinCellsSufficient affinityMARCKSAssaysPhosphorylationSubstratePhenotypeSV40
1985
Identification of calmodulin-dependent protein kinase III and its major Mr 100,000 substrate in mammalian tissues.
Nairn A, Bhagat B, Palfrey H. Identification of calmodulin-dependent protein kinase III and its major Mr 100,000 substrate in mammalian tissues. Proceedings Of The National Academy Of Sciences Of The United States Of America 1985, 82: 7939-7943. PMID: 3906654, PMCID: PMC390885, DOI: 10.1073/pnas.82.23.7939.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCalmodulin-Binding ProteinsCell LineCytosolImmunosorbent TechniquesMolecular WeightPancreasProtein KinasesRatsSubstrate SpecificityTissue DistributionConceptsCaM-dependent protein kinaseCaM kinase IIIKinase IIIProtein kinaseMammalian tissuesCalmodulin-dependent protein kinase IIIProtein kinase IIIDependent protein kinaseProtein phosphorylation systemsWidespread tissue distributionTotal cytosolic proteinAnimal cellsPhosphorylation systemSubstrate specificityCytosolic proteinsMyosin light chainMajor substrateKinaseProteinSynapsin IPoor substrateCell linesPhosphorylase bMajor MrPolyclonal antibodies