2005
A molecular switch for translational control in taste memory consolidation
Belelovsky K, Elkobi A, Kaphzan H, Nairn A, Rosenblum K. A molecular switch for translational control in taste memory consolidation. European Journal Of Neuroscience 2005, 22: 2560-2568. PMID: 16307598, DOI: 10.1111/j.1460-9568.2005.04428.x.Peer-Reviewed Original ResearchConceptsEukaryotic elongation factor 2Protein synthesisEEF2 phosphorylationKinase 2 activationElongation factor 2Translational regulationTranslation initiationTranslational controlS6K1 phosphorylationMolecular switchSwitch-like effectNeuronal proteinsPhosphorylationElongation rateRate-limiting stepFactor 2Taste memory consolidationSynaptoneurosomal fractionsExpressionTemporal patternsInitiation rateProtein
2001
Auto‐inhibition of Ca2+/calmodulin‐dependent protein kinase II by its ATP‐binding domain
Lengyel I, Nairn A, McCluskey A, Tóth G, Penke B, Rostas J. Auto‐inhibition of Ca2+/calmodulin‐dependent protein kinase II by its ATP‐binding domain. Journal Of Neurochemistry 2001, 76: 1066-1072. PMID: 11181826, DOI: 10.1046/j.1471-4159.2001.00139.x.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAnimalsBinding SitesCalcium-Calmodulin-Dependent Protein Kinase Type 1Calcium-Calmodulin-Dependent Protein Kinase Type 2Calcium-Calmodulin-Dependent Protein Kinase Type 4Calcium-Calmodulin-Dependent Protein KinasesCyclic AMP-Dependent Protein KinasesDose-Response Relationship, DrugEnzyme ActivationEnzyme InhibitorsPeptide FragmentsPeptidesProtein Structure, TertiaryRatsSubstrate SpecificityConceptsATP-binding domainDependent protein kinase IIProtein kinase IIProtein kinaseCaMPK-IIKinase IICAMP-dependent protein kinaseDependent protein kinaseSubstitution of phenylalaninePhysiological processesKey enzymeAutocamtide-2Position 25Phenylalanine 25Molecular interactionsKinasePeptide fragmentsDependent activityIndependent activityATPEnzymeCrucial roleIntramolecular interactionsDomainInhibition
2000
The Dopamine/D1 Receptor Mediates the Phosphorylation and Inactivation of the Protein Tyrosine Phosphatase STEP via a PKA-Dependent Pathway
Paul S, Snyder G, Yokakura H, Picciotto M, Nairn A, Lombroso P. The Dopamine/D1 Receptor Mediates the Phosphorylation and Inactivation of the Protein Tyrosine Phosphatase STEP via a PKA-Dependent Pathway. Journal Of Neuroscience 2000, 20: 5630-5638. PMID: 10908600, PMCID: PMC6772528, DOI: 10.1523/jneurosci.20-15-05630.2000.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAnimalsCatalytic DomainCorpus StriatumCyclic AMP-Dependent Protein KinasesEnzyme ActivationIn Vitro TechniquesMaleMolecular Sequence DataNeuronsPhosphoproteinsPhosphorus RadioisotopesPhosphorylationProtein Tyrosine PhosphatasesProtein Tyrosine Phosphatases, Non-ReceptorRatsRats, Sprague-DawleyReceptors, Dopamine D1Signal TransductionConceptsProtein tyrosine phosphatase familyCAMP-dependent protein kinaseTryptic phosphopeptide mappingPotential phosphorylation sitesUnique N-terminalProtein-protein interactionsMembrane-associated proteinsRole of phosphorylationTyrosine phosphatase familyAmino acid sequenceSite-directed mutagenesisAmino acid sequencingPKA-dependent pathwayTyrosine phosphatase STEPPhosphatase familyPhosphopeptide mappingPhosphorylation sitesAlternative splicingSubcellular compartmentsProtein kinaseTerminal domainEquivalent residuesCytosolic proteinsSpecific residuesAcid sequence
1998
Ca2+/calmodulin-dependent kinase II mediates simultaneous enhancement of gap-junctional conductance and glutamatergic transmission
Pereda A, Bell T, Chang B, Czernik A, Nairn A, Soderling T, Faber D. Ca2+/calmodulin-dependent kinase II mediates simultaneous enhancement of gap-junctional conductance and glutamatergic transmission. Proceedings Of The National Academy Of Sciences Of The United States Of America 1998, 95: 13272-13277. PMID: 9789078, PMCID: PMC23780, DOI: 10.1073/pnas.95.22.13272.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBenzylaminesCalciumCalcium ChlorideCalcium-Calmodulin-Dependent Protein Kinase Type 2Calcium-Calmodulin-Dependent Protein KinasesCell CommunicationDendritesEgtazic AcidElectric ConductivityElectric StimulationEnzyme ActivationEnzyme InhibitorsEvoked PotentialsExcitatory Postsynaptic PotentialsGap JunctionsGlutamic AcidGoldfishMembrane PotentialsNeuronsSpinal CordSulfonamidesSynapsesSynaptic TransmissionVestibulocochlear NerveConceptsGlutamatergic synapsesGap junctional conductanceCaM-KIIGap junctionsLong-term potentiationGoldfish Mauthner cellIntradendritic Ca2Intradendritic injectionPostsynaptic increaseExcitatory transmissionGlutamatergic transmissionAuditory afferentsSynaptic responsesSynaptic activityDependent kinase inhibitorDependent kinase IIIntracellular Ca2Interneuronal communicationSpecific peptide inhibitorChemical synapsesKinase inhibitorsMauthner cellKN-93Mammalian glutamatergic synapsesSynapsesCharacterization of the Mechanism of Regulation of Ca2+/ Calmodulin-dependent Protein Kinase I by Calmodulin and by Ca2+/Calmodulin-dependent Protein Kinase Kinase*
Matsushita M, Nairn A. Characterization of the Mechanism of Regulation of Ca2+/ Calmodulin-dependent Protein Kinase I by Calmodulin and by Ca2+/Calmodulin-dependent Protein Kinase Kinase*. Journal Of Biological Chemistry 1998, 273: 21473-21481. PMID: 9705275, DOI: 10.1074/jbc.273.34.21473.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsCalcium-Calmodulin-Dependent Protein Kinase KinaseCalcium-Calmodulin-Dependent Protein Kinase Type 1Calcium-Calmodulin-Dependent Protein Kinase Type 4Calcium-Calmodulin-Dependent Protein KinasesCalmodulinCloning, MolecularEnzyme ActivationKineticsMolecular Sequence DataPhosphorylationProtein Serine-Threonine KinasesRatsConceptsProtein kinase IAbsence of CaMKinase ICalmodulin-dependent protein kinase IDetailed structure-function analysisDependent protein kinase IDependent protein kinase kinaseProtein kinase kinaseStructure-function analysisMechanism of regulationSpecific amino acidsEnzyme activityKinase kinaseAutoinhibited stateRegulatory domainCatalytic coreCaMKIMutant formsBasal enzyme activitySecond enzymeCaMKKAmino acidsAdditional mutationsMutationsActive formRegulation of Secretion of Alzheimer Amyloid Precursor Protein by the Mitogen‐Activated Protein Kinase Cascade
Desdouits‐Magnen J, Desdouits F, Takeda S, Syu L, Saltiel A, Buxbaum J, Czernik A, Nairn A, Greengard P. Regulation of Secretion of Alzheimer Amyloid Precursor Protein by the Mitogen‐Activated Protein Kinase Cascade. Journal Of Neurochemistry 1998, 70: 524-530. PMID: 9453546, DOI: 10.1046/j.1471-4159.1998.70020524.x.Peer-Reviewed Original ResearchMeSH KeywordsAmyloid beta-PeptidesAmyloid beta-Protein PrecursorAnimalsCalcium-Calmodulin-Dependent Protein KinasesCarbacholCHO CellsCOS CellsCricetinaeEnzyme ActivationEnzyme InhibitorsFlavonoidsHumansIndolesMaleimidesMitogen-Activated Protein Kinase KinasesMuscarinic AgonistsNerve Growth FactorsPC12 CellsPhorbol 12,13-DibutyrateProtein Kinase InhibitorsProtein KinasesRatsReceptor, Muscarinic M1Receptors, MuscarinicConceptsProtein kinase CAlzheimer amyloid precursor proteinKinase cascadeM1 muscarinic receptor stimulationMitogen-Activated Protein Kinase CascadeProtein kinase cascadeMAP kinase cascadeMAP kinase kinaseMAP kinase-independent pathwayMitogen-activated protein kinase kinase activationDominant negative mutantPrecursor proteinDistinct secretory pathwaysPKC-independent pathwayStimulation of PKCAmyloid precursor proteinKinase-independent pathwaySAPP secretionKinase kinaseSecretory pathwayNegative mutantMAP kinaseKinase activationRegulation of secretionPD 98059
1997
Regulation of rat Na+-K+-ATPase activity by PKC is modulated by state of phosphorylation of Ser-943 by PKA
Cheng X, Höög J, Nairn A, Greengard P, Aperia A. Regulation of rat Na+-K+-ATPase activity by PKC is modulated by state of phosphorylation of Ser-943 by PKA. American Journal Of Physiology 1997, 273: c1981-c1986. PMID: 9435504, DOI: 10.1152/ajpcell.1997.273.6.c1981.Peer-Reviewed Original ResearchMeSH KeywordsAlanineAmino Acid SubstitutionAnimalsColforsinCOS CellsCyclic AMPCyclic AMP-Dependent Protein KinasesCytosolDichlororibofuranosylbenzimidazoleEnzyme ActivationHomeostasisIsoenzymesKineticsMutagenesis, Site-DirectedPhorbol 12,13-DibutyratePhosphorylationProtein Kinase CRatsRecombinant ProteinsSerineSodium-Potassium-Exchanging ATPaseThionucleotidesTransfectionConceptsProtein kinase AProtein kinase CATPase alpha 1State of phosphorylationEffect of PKCWild-type enzymeSpecific PKA activatorActivity of PKCEnzyme activityAlpha 1Direct phosphorylationCOS cellsATPase alphaKinase ASer-23Kinase CPKA activatorPhosphorylationPKA systemPhorbol esterATPase activityMutantsEffect of PDBuCellsInhibition
1996
Activation of a Calcium-Calmodulin-dependent Protein Kinase I Cascade in PC12 Cells*
Aletta J, Selbert M, Nairn A, Edelman A. Activation of a Calcium-Calmodulin-dependent Protein Kinase I Cascade in PC12 Cells*. Journal Of Biological Chemistry 1996, 271: 20930-20934. PMID: 8702851, DOI: 10.1074/jbc.271.34.20930.Peer-Reviewed Original ResearchConceptsCaM kinase IDependent protein kinase IKinase IProtein kinase IPC12 cellsIntracellular Ca2L-type voltage-dependent Ca2PC12 pheochromocytoma cellsBlockade of Ca2Cellular regulationBiphasic phosphorylationVoltage-dependent Ca2Depolarization-induced activationPhosphorylationCalcium-calmodulinActivity of Ca2Extracellular Ca2I activityAcute formPheochromocytoma cellsPrior depolarizationIntracellular phosphorylationCellsActivationCa2Structure, Regulation, and Function of Calcium/Calmodulin-Dependent Protein Kinase I
Picciotto M, Nastiuk K, Nairn A. Structure, Regulation, and Function of Calcium/Calmodulin-Dependent Protein Kinase I. Advances In Pharmacology 1996, 36: 251-275. PMID: 8783563, DOI: 10.1016/s1054-3589(08)60585-2.Peer-Reviewed Original ResearchConceptsProtein kinaseProtein kinase CMyosin light chain kinaseKinase ICaM kinaseSecond messenger-regulated protein kinasesCalmodulin-dependent protein kinase ICalcium/calmodulin-dependent protein kinase ICAMP-dependent protein kinaseSpecific subcellular locationsMultifunctional protein kinaseTerminal regulatory domainDependent protein kinaseCaM kinase familyClass of enzymesProtein kinase ICaM kinase IAmino acid residuesMyosin P-light chainDomain bindsAutoinhibitory mechanismRegulatory domainKinase familyProtein phosphorylationLight chain kinase
1991
Regulation by phosphorylation of reversible association of a myristoylated protein kinase C substrate with the plasma membrane
Thelen M, Rosen A, Nairn A, Aderem A. Regulation by phosphorylation of reversible association of a myristoylated protein kinase C substrate with the plasma membrane. Nature 1991, 351: 320-322. PMID: 2034276, DOI: 10.1038/351320a0.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAutoradiographyCell MembraneEnzyme ActivationEthers, CyclicHumansIntracellular Signaling Peptides and ProteinsKineticsMembrane ProteinsMyristic AcidMyristic AcidsMyristoylated Alanine-Rich C Kinase SubstrateNeutrophilsN-Formylmethionine Leucyl-PhenylalanineOkadaic AcidPhosphorus RadioisotopesPhosphorylationProtein Kinase CProteinsTritiumConceptsProtein kinase CProtein kinase C substrateAlanine-rich C kinase substrateActin-membrane interactionsMembrane-bound substratesActin-binding proteinsSpecific PKC substrateC kinase substrateReceptor-mediated signalsMembrane targetingKinase substrateMembrane attachmentPKC substratePlasma membraneSubsequent dephosphorylationKinase CC substrateMARCKSNovel mechanismReversible associationProteinMembraneEffective bindingMyristoylationMacrophage activation
1990
Activation of protein kinase C results in the displacement of its myristoylated, alanine-rich substrate from punctate structures in macrophage filopodia.
Rosen A, Keenan K, Thelen M, Nairn A, Aderem A. Activation of protein kinase C results in the displacement of its myristoylated, alanine-rich substrate from punctate structures in macrophage filopodia. Journal Of Experimental Medicine 1990, 172: 1211-1215. PMID: 2212950, PMCID: PMC2188604, DOI: 10.1084/jem.172.4.1211.Peer-Reviewed Original ResearchConceptsProtein kinase CPKC-dependent phosphorylationPhosphorylation-dependent releaseProtein kinase C resultsAlanine-rich C kinase substrateDiverse cellular processesC kinase substrateCell-substratum interfacePhorbol esters resultsActivation of PKCPunctate stainingKinase substrateCellular processesProminent substratePunctate structuresMembrane cytoskeletonLoss of filopodiaPlasma membranePunctate distributionVariety of cellsCell spreadingMARCKSKinase CMacrophage filopodiaFilopodiaNerve Growth Factor‐Induced Down‐Regulation of Calmodulin‐Dependent Protein Kinase III in PC12 Cells Involves Cyclic AMP‐Dependent Protein Kinase
Brady M, Nairn A, Wagner J, Palfrey H. Nerve Growth Factor‐Induced Down‐Regulation of Calmodulin‐Dependent Protein Kinase III in PC12 Cells Involves Cyclic AMP‐Dependent Protein Kinase. Journal Of Neurochemistry 1990, 54: 1034-1039. PMID: 1689374, DOI: 10.1111/j.1471-4159.1990.tb02354.x.Peer-Reviewed Original ResearchConceptsWild-type cellsCalmodulin-dependent protein kinase IIICAMP-dependent protein kinase activityProtein kinase IIIProtein kinase activityEpidermal growth factorKinase IIIKinase activityA126-1B2 cellsCyclic AMP-dependent protein kinaseAMP-dependent protein kinasePC12 cellsNerve growth factorMutant PC12 cell lineElongation factor 2Growth factorAbility of NGFPC12 cell lineEffects of NGFProtein kinaseNGF additionA126-1B2Down regulationCell linesFactor 2Role of Ca2+/calmodulin-dependent protein phosphorylation in signal transduction.
Nairn A. Role of Ca2+/calmodulin-dependent protein phosphorylation in signal transduction. 1990, 24: 202-5. PMID: 1976329.Peer-Reviewed Original Research
1989
Regulation of Chloride Channels by Protein Kinase C in Normal and Cystic Fibrosis Airway Epithelia
Li M, McCann J, Anderson M, Clancy J, Liedtke C, Nairn A, Greengard P, Welsch M. Regulation of Chloride Channels by Protein Kinase C in Normal and Cystic Fibrosis Airway Epithelia. Science 1989, 244: 1353-1356. PMID: 2472006, DOI: 10.1126/science.2472006.Peer-Reviewed Original ResearchConceptsProtein kinase CChloride channelsKinase CApical membrane chloride channelMembrane chloride channelCystic fibrosis cellsMembrane proteinsCell-free membraneCystic fibrosis airway epitheliaChloride secretionIntact cellsPhorbol esterPhysiological statusDefective regulationAirway epithelial cellsEpithelial cellsCellsRegulationChannel inactivationCystic fibrosisActivationCalcium concentrationLow calcium concentrationsProteinAirway epithelium
1988
Autophosphorylation and activation of Ca2+/calmodulin-dependent protein kinase II in intact nerve terminals.
Gorelick FS, Wang JK, Lai Y, Nairn AC, Greengard P. Autophosphorylation and activation of Ca2+/calmodulin-dependent protein kinase II in intact nerve terminals. Journal Of Biological Chemistry 1988, 263: 17209-17212. PMID: 2846557, DOI: 10.1016/s0021-9258(19)77816-8.Peer-Reviewed Original ResearchConceptsDependent protein kinase IIKinase IIAlpha subunitProtein kinase IIKinase II activityTwo-dimensional phosphopeptide mapsII activityState of phosphorylationAutophosphorylation mechanismThreonine residuesPhosphothreonine contentPhosphopeptide mapsTransient phosphorylationIndependent speciesPhosphoserine contentIntact nerve terminalsBeta subunitEnhanced phosphorylationSubunitsPhosphorylationAutophosphorylationIntact synaptosomesBasal incubation conditionsPhosphopeptidesDepolarization of synaptosomes
1987
Rapid activation of calmodulin-dependent protein kinase III in mitogen-stimulated human fibroblasts. Correlation with intracellular Ca2+ transients.
Palfrey H, Nairn A, Muldoon L, Villereal M. Rapid activation of calmodulin-dependent protein kinase III in mitogen-stimulated human fibroblasts. Correlation with intracellular Ca2+ transients. Journal Of Biological Chemistry 1987, 262: 9785-9792. PMID: 3496338, DOI: 10.1016/s0021-9258(18)48002-7.Peer-Reviewed Original ResearchCholecystokinin induces a decrease in Ca2+ current in snail neurons that appears to be mediated by protein kinase C
Hammond C, Paupardin-Tritsch D, Nairn A, Greengard P, Gerschenfeld H. Cholecystokinin induces a decrease in Ca2+ current in snail neurons that appears to be mediated by protein kinase C. Nature 1987, 325: 809-811. PMID: 2434859, DOI: 10.1038/325809a0.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCalciumEgtazic AcidElectric ConductivityEnzyme ActivationHelix, SnailsIon ChannelsNeuronsProtein Kinase CSincalideConceptsProtein kinase CAction of noradrenalineDependent action potentialsKinase CIntracellular injectionSnail neuronsAction potentialsProtein kinaseCardiac muscleCholecystokininSnail Helix aspersaExcitable tissuesProtein kinase C.Low concentrationsCa2Cyclic GMP-dependent protein kinaseHelix aspersaInjectionGMP-dependent protein kinaseKinase C.KinaseNoradrenalineCCK8Neurons
1986
cGMP-dependent protein kinase enhances Ca2+ current and potentiates the serotonin-induced Ca2+ current increase in snail neurones
Paupardin-Tritsch D, Hammond C, Gerschenfeld H, Nairn A, Greengard P. cGMP-dependent protein kinase enhances Ca2+ current and potentiates the serotonin-induced Ca2+ current increase in snail neurones. Nature 1986, 323: 812-814. PMID: 3022154, DOI: 10.1038/323812a0.Peer-Reviewed Original ResearchConceptsIntracellular injectionCyclic GMP-dependent protein kinaseNeuronal membrane permeabilityAbsence of serotoninProtein kinaseSynaptic transmissionNeuronal functionIncrease of Ca2NeuronesCGMP-dependent protein kinaseGMP-dependent protein kinaseSerotoninSnail neuronesCyclic AMPMembrane permeabilityInjectionPhysiological roleProtein phosphorylationCa2CGMPKinase
1980
The preparation of calmodulins from barley (Hordeum sp.) and basidiomycete fungi
Grand R, Nairn A, Perry S. The preparation of calmodulins from barley (Hordeum sp.) and basidiomycete fungi. Biochemical Journal 1980, 185: 755-760. PMID: 6248033, PMCID: PMC1161454, DOI: 10.1042/bj1850755.Peer-Reviewed Original ResearchConceptsRabbit skeletal muscle troponin ICalmodulin-like proteinPresence of Ca2Myosin light chain kinaseSkeletal muscle troponin IMammalian proteinsFungal calmodulinsLight chain kinaseMammalian calmodulinBovine brain calmodulinHigher fungiAmino acid analysisEscherichia coliCalmodulinProteinFungiE. coliAcid analysisBrain calmodulinElectrophoretic mobilityBarleyPolyacrylamide gelsM ureaColiNumber of differences
1979
Calmodulin and myosin light-chain kinase of rabbit fast skeletal muscle
Nairn A, Perry S. Calmodulin and myosin light-chain kinase of rabbit fast skeletal muscle. Biochemical Journal 1979, 179: 89-97. PMID: 224861, PMCID: PMC1186598, DOI: 10.1042/bj1790089.Peer-Reviewed Original Research