1999
The expression of Ca2+/calmodulin-dependent protein kinase I in rat retina is regulated by light stimulation
Tsumura T, Murata A, Yamaguchi F, Sugimoto K, Hasegawa E, Hatase O, Nairn A, Tokuda M. The expression of Ca2+/calmodulin-dependent protein kinase I in rat retina is regulated by light stimulation. Vision Research 1999, 39: 3165-3173. PMID: 10615488, DOI: 10.1016/s0042-6989(99)00063-2.Peer-Reviewed Original ResearchInhibition of the Ca2+/Calmodulin-dependent Protein Kinase I Cascade by cAMP-dependent Protein Kinase*
Matsushita M, Nairn A. Inhibition of the Ca2+/Calmodulin-dependent Protein Kinase I Cascade by cAMP-dependent Protein Kinase*. Journal Of Biological Chemistry 1999, 274: 10086-10093. PMID: 10187789, DOI: 10.1074/jbc.274.15.10086.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCalcium-Calmodulin-Dependent Protein Kinase KinaseCalcium-Calmodulin-Dependent Protein Kinase Type 1Calcium-Calmodulin-Dependent Protein Kinase Type 4Calcium-Calmodulin-Dependent Protein KinasesCyclic AMP-Dependent Protein KinasesFeedbackHippocampusPC12 CellsPeptide MappingPhosphorylationProtein Serine-Threonine KinasesRatsSubstrate SpecificityConceptsActivation of PKACAMP-dependent protein kinaseDependent protein kinase IProtein kinaseProtein kinase IThreonine 108Kinase ITwo-dimensional phosphopeptide mappingDependent signal transduction pathwaysInhibition of CaMKKSignal transduction pathwaysIntact PC12 cellsRegulatory phosphorylationPhosphopeptide mappingTransduction pathwaysCaMKI activityCaMKKIntact cellsPhosphorylationPC12 cellsKinaseNegative feedback mechanismEnzyme cascadeEnzyme activityRapid inhibition
1998
Characterization 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 formCellular Localization of Calmodulin-dependent Protein Kinases I and II to A-cells and D-cells of the Endocrine Pancreas
Matovcik L, Nairn A, Gorelick F. Cellular Localization of Calmodulin-dependent Protein Kinases I and II to A-cells and D-cells of the Endocrine Pancreas. Journal Of Histochemistry & Cytochemistry 1998, 46: 519-526. PMID: 9524198, DOI: 10.1177/002215549804600412.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCalcium-Calmodulin-Dependent Protein Kinase Type 1Calcium-Calmodulin-Dependent Protein Kinase Type 2Calcium-Calmodulin-Dependent Protein KinasesCyclic AMP Response Element-Binding ProteinCystic Fibrosis Transmembrane Conductance RegulatorDigestive SystemFluorescent Antibody Technique, IndirectGlucagonImmunoblottingIslets of LangerhansMicroscopy, ConfocalPancreasRatsSomatostatinSomatostatin-Secreting CellsTissue DistributionConceptsCaM kinase IKinase IProtein kinase ICaM kinase IIGlucagon secretionKinase IICalmodulin-dependent protein kinase ISomatostatin cellsDependent protein kinase IA cellsSomatostatin-containing D-cellsD cellsDifferent cell typesRegulation of Ca2Islets of LangerhansCaM kinaseCytosolic proteinsI antibodiesSomatostatin granulesPancreatic polypeptideCellular localizationRegulatory rolePeptide antibodiesIntracellular Ca2Endocrine pancreas
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 phosphorylationCellsActivationCa2cGMP-Dependent Protein Kinase in Dorsal Root Ganglion: Relationship with Nitric Oxide Synthase and Nociceptive Neurons
Qian Y, Chao D, Santillano D, Cornwell T, Nairn A, Greengard P, Lincoln T, Bredt D. cGMP-Dependent Protein Kinase in Dorsal Root Ganglion: Relationship with Nitric Oxide Synthase and Nociceptive Neurons. Journal Of Neuroscience 1996, 16: 3130-3138. PMID: 8627352, PMCID: PMC6579134, DOI: 10.1523/jneurosci.16-10-03130.1996.Peer-Reviewed Original ResearchConceptsNeuronal nitric oxide synthaseCGMP-dependent protein kinaseNitric oxide synthaseSensory neuronsProtein kinase ICGMP-dependent protein kinase IOxide synthaseKinase IEmbryonic developmentProtein kinaseG-substrateCalcitonin gene-related polypeptideMedium-diameter DRG neuronsPeripheral nerve axotomyInfluences plasticityDorsal root gangliaCGMP actionRoof plateNerve axotomyDRG neuronsNociceptive neuronsNociceptive processingRoot gangliaSubstance PSpinal cordStructural Basis for the Autoinhibition of Calcium/Calmodulin-Dependent Protein Kinase I
Goldberg J, Nairn A, Kuriyan J. Structural Basis for the Autoinhibition of Calcium/Calmodulin-Dependent Protein Kinase I. Cell 1996, 84: 875-887. PMID: 8601311, DOI: 10.1016/s0092-8674(00)81066-1.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAnimalsBinding SitesCalcium-Calmodulin-Dependent Protein Kinase Type 1Calcium-Calmodulin-Dependent Protein KinasesCrystallographyImage Processing, Computer-AssistedMolecular Sequence DataPhosphorylationProtein ConformationProtein KinasesRatsSequence Homology, Amino AcidSubstrate SpecificityConceptsCalmodulin-dependent protein kinase ICalcium/calmodulin-dependent protein kinase IProtein kinase IKinase IRegulatory regionsATP-binding domainTerminal regulatory regionCatalytic domainCatalytic coreSecond helixStructural basisAlpha-helixCalmodulin targetsConformational changesPeptide substratesHelix segmentsCalmodulinHelixSubstantial structural changesRecognition elementInitial interactionInhibitory interactionsDomainAutoinhibitionCrystal structureStructure, 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
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-transferaseImmunochemical localization of calcium/calmodulin‐dependent protein kinase I
Picciotto M, Zoli M, Bertuzzi G, Nairn A. Immunochemical localization of calcium/calmodulin‐dependent protein kinase I. Synapse 1995, 20: 75-84. PMID: 7624832, DOI: 10.1002/syn.890200111.Peer-Reviewed Original ResearchConceptsKinase IProtein kinase ICaM kinase INon-neuronal tissuesImmunoreactive speciesCalmodulin-dependent protein kinase IGlutathione S-transferase fusion proteinCalcium/calmodulin-dependent protein kinase IRat brainDependent protein kinase ISubcellular fractionation studiesRecombinant kinasesRat brain enzymeNeuronal cell bodiesCytosolic localizationProtein kinaseMultiple immunoreactive speciesMajor immunoreactive speciesFusion proteinMultiple neuronal processesWidespread cellMajor immunoreactive bandRat cDNAPrimary structureSynapsin I.CaMKI CaM-dependent protein kinase I (vertebrates)
Edelman A, Nairn A. CaMKI CaM-dependent protein kinase I (vertebrates). 1995, 128-130. DOI: 10.1016/b978-012324719-3/50029-7.Peer-Reviewed Original ResearchCystic fibrosis transmembrane conductance regulatorKinase IProtein kinase ICaM kinase ICAMP response element-binding proteinCaM-dependent protein kinase ICalmodulin-dependent protein kinase IPartial amino acid sequence dataShort N-terminal extensionLong C-terminal extensionAmino acid sequence dataFibrosis transmembrane conductance regulatorN-terminal extensionC-terminal extensionCaM-binding domainSynaptic vesicle functionAmino acid sequenceBrain cDNA libraryRat brain cDNA libraryTransmembrane conductance regulatorWidespread tissue distributionResponse element-binding proteinElement-binding proteinIon channel activityKinase domainP3-52 IDENTIFICATION OF AUTOINHIBITORY AND CALMODULIN-RINDING DOMAINS ON CALCIUM/CALMODULIN-DEPENDENT PROTEIN KINASE I
Yokokura H, Picciotto M, Nairn A, Hidaka H. P3-52 IDENTIFICATION OF AUTOINHIBITORY AND CALMODULIN-RINDING DOMAINS ON CALCIUM/CALMODULIN-DEPENDENT PROTEIN KINASE I. Journal Of Pharmacological Sciences 1995, 67: 259. DOI: 10.1016/s0021-5198(19)47002-9.Peer-Reviewed Original Research
1991
Protein kinase C substrate and inhibitor characteristics of peptides derived from the myristoylated alanine-rich C kinase substrate (MARCKS) protein phosphorylation site domain
Graff J, Rajan R, Randall R, Nairn A, Blackshear P. Protein kinase C substrate and inhibitor characteristics of peptides derived from the myristoylated alanine-rich C kinase substrate (MARCKS) protein phosphorylation site domain. Journal Of Biological Chemistry 1991, 266: 14390-14398. PMID: 1650359, DOI: 10.1016/s0021-9258(18)98697-7.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceCalcium-Calmodulin-Dependent Protein KinasesIntracellular Signaling Peptides and ProteinsMembrane ProteinsMolecular Sequence DataMyristoylated Alanine-Rich C Kinase SubstratePeptidesPhosphopeptidesPhosphorylationProtein Kinase CProtein KinasesProteinsSerineSubstrate SpecificityTrypsinConceptsProtein kinase CCGMP-dependent protein kinasePhosphorylation site domainCatalytic fragmentKinase CProtein kinaseSite domainProtein kinase C substrateProtein kinase C phosphorylationDependent protein kinase IAlanine-rich C kinase substrateKinase C phosphorylationC kinase substrateProtein kinase IProtein kinase IIHigh-affinity substrateKinase substratePhosphorylation sitesTryptic phosphopeptidesKinase IBasic regionMARCKS proteinProtein consistC phosphorylationKinase II
1989
Identification of two protein kinases that phosphorylate the neural cell-adhesion molecule, N-CAM
Mackie K, Sorkin B, Nairn A, Greengard P, Edelman G, Cunningham B. Identification of two protein kinases that phosphorylate the neural cell-adhesion molecule, N-CAM. Journal Of Neuroscience 1989, 9: 1883-1896. PMID: 2542481, PMCID: PMC6569722, DOI: 10.1523/jneurosci.09-06-01883.1989.Peer-Reviewed Original ResearchConceptsProtein kinaseLarge polypeptidesCytoplasmic domainKinase ICell adhesion moleculeNeural cell adhesion moleculeThreonyl residuesCalmodulin-dependent protein kinase IN-CAMCalcium/calmodulin-dependent protein kinase ICyclic AMP-dependent protein kinaseCyclic GMP-dependent protein kinaseGlycogen synthase kinase-3AMP-dependent protein kinaseCommon phosphorylation sitesGMP-dependent protein kinaseCasein kinase IISynthase kinase-3Protein kinase IN-CAM polypeptidesChicken N-CAMProtein kinase CPrior phosphorylationPhosphorylation sitesAlternative splicing