2001
Mechanisms for Increased Levels of Phosphorylation of Elongation Factor-2 during Hibernation in Ground Squirrels †
Chen Y, Matsushita M, Nairn A, Damuni Z, Cai D, Frerichs K, Hallenbeck J. Mechanisms for Increased Levels of Phosphorylation of Elongation Factor-2 during Hibernation in Ground Squirrels †. Biochemistry 2001, 40: 11565-11570. PMID: 11560506, DOI: 10.1021/bi010649w.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBrainCalcium-Calmodulin-Dependent Protein KinasesCatalysisCytosolElongation Factor 2 KinaseHibernationLiverPeptide Elongation Factor 2Phosphoprotein PhosphatasesPhosphorylationProtein Phosphatase 2Protein SubunitsSciuridaeConceptsEukaryotic elongation factor 2EEF-2 phosphorylationElongation factor 2Elongation phaseEEF-2 kinase activityProtein phosphatase 2AGround squirrelsLevel of phosphorylationFactor 2Phosphatase 2ACellular functionsCatalytic subunitUncharacterized mechanismKinase activityInhibitor 2Protein synthesisPhosphorylationPP2AHibernating animalsActive animalsHibernatorsReversible mechanismSevere reductionSquirrelsHibernationAuto‐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 interactionsDomainInhibitionElongation Factor-2 Phosphorylation and the Regulation of Protein Synthesis by Calcium
Nairn A, Matsushita M, Nastiuk K, Horiuchi A, Mitsui K, Shimizu Y, Palfrey H. Elongation Factor-2 Phosphorylation and the Regulation of Protein Synthesis by Calcium. Progress In Molecular And Subcellular Biology 2001, 27: 91-129. PMID: 11575162, DOI: 10.1007/978-3-662-09889-9_4.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsCalciumCalcium-Calmodulin-Dependent Protein KinasesCell CycleCell DivisionCyclic AMP-Dependent Protein KinasesCysteine EndopeptidasesElongation Factor 2 KinaseHumansMolecular Sequence DataMultienzyme ComplexesNeuronsPeptide Chain Elongation, TranslationalPeptide Elongation Factor 2PhosphorylationProteasome Endopeptidase ComplexProtein BiosynthesisSequence Homology, Amino AcidSignal TransductionUbiquitinConceptsProtein synthesisElongation factor 2 phosphorylationDephosphorylation of eEF2Eukaryotic protein synthesisAminoacyl-tRNA synthetasesFactor 2 phosphorylationElongation factor 2Ribosomal proteinsRegulated processInitiation factorsDependent kinasesKey proteinsRate of elongationPeptidyl-tRNAPhysiological roleKinasePhosphorylationFactor 2EEF2P siteThr56ProteinSynthetasesDephosphorylationRibosomes
2000
Novel compounds, ‘1,3-selenazine derivatives’ as specific inhibitors of eukaryotic elongation factor-2 kinase
Cho S, Koketsu M, Ishihara H, Matsushita M, Nairn A, Fukazawa H, Uehara Y. Novel compounds, ‘1,3-selenazine derivatives’ as specific inhibitors of eukaryotic elongation factor-2 kinase. Biochimica Et Biophysica Acta 2000, 1475: 207-215. PMID: 10913818, DOI: 10.1016/s0304-4165(00)00061-1.Peer-Reviewed Original ResearchMeSH Keywords3T3 CellsAcetophenonesAnimalsBenzopyransCalcium-Calmodulin-Dependent Protein KinasesCloning, MolecularElongation Factor 2 KinaseEnzyme InhibitorsMiceMolecular StructureOrganoselenium CompoundsConceptsV-src-transformed NIH3T3 cellsEukaryotic elongation factor 2 kinaseProtein kinase AElongation factor 2 kinaseProtein kinase CProtein tyrosine kinasesEEF-2KProtein kinaseEEF-2K inhibitorNIH3T3 cellsCalmodulin-dependent protein kinaseV-Src kinaseMultiple protein kinasesCalmodulin-dependent protein kinase IIProtein levelsK inhibitorsProtein kinase IIEEF-2K.Kinase AKinase IITyrosine kinaseKinase CKinaseTs-4Specific inhibitorNMDA receptor-mediated control of protein synthesis at developing synapses
Scheetz A, Nairn A, Constantine-Paton M. NMDA receptor-mediated control of protein synthesis at developing synapses. Nature Neuroscience 2000, 3: 211-216. PMID: 10700251, DOI: 10.1038/72915.Peer-Reviewed Original ResearchMeSH Keywords2-Amino-5-phosphonovalerateAnimalsCalcium-Calmodulin-Dependent Protein Kinase Type 2Calcium-Calmodulin-Dependent Protein KinasesCycloheximideElectrophoresis, Gel, Two-DimensionalGlutamic AcidIsoelectric PointMolecular WeightN-MethylaspartatePeptide Elongation Factor 2PhosphorylationPrecipitin TestsProtein BiosynthesisProteinsRatsReceptors, N-Methyl-D-AspartateRetinal Ganglion CellsSuperior ColliculiSynapsesSynaptosomesTime FactorsConceptsNMDAR activationReceptor activationN-methyl-D-aspartate (NMDA) receptor activationActivity-dependent synaptic changesEukaryotic elongation factor 2Receptor-mediated controlSynaptic protein synthesisEEF2 phosphorylationProtein synthesisSuperior colliculiYoung ratsDependent kinase IISynaptic changesLow dosesTotal protein synthesisII synthesisFactor 2Overall protein synthesisActivationElongation factor 2Kinase IIPhosphorylation
1999
Modulation of a calcium/calmodulin-dependent protein kinase cascade by retinoic acid during neutrophil maturation
Lawson N, Zain M, Zibello T, Picciotto M, Nairn A, Berliner N. Modulation of a calcium/calmodulin-dependent protein kinase cascade by retinoic acid during neutrophil maturation. Experimental Hematology 1999, 27: 1682-1690. PMID: 10560916, DOI: 10.1016/s0301-472x(99)00108-3.Peer-Reviewed Original ResearchMeSH KeywordsCalcium-Calmodulin-Dependent Protein KinasesCell LineCellular SenescenceDNA, ComplementaryNeutrophilsTretinoinConceptsKinase cascadeCaM kinase cascadeNeutrophil maturationRetinoic acidDependent protein kinase kinase alphaWestern analysisProtein kinase cascadeSpecific gene expressionImmediate early fashionNeutrophil-specific gene expressionTrans retinoic acidNeutrophil progenitor cellsRetinoic acid receptorsNeutrophil functionUninduced cellsGene expressionKinase alphaMyeloid cellsVitamin AAcid receptorsRetinoid signalingCell typesEffect of calciumProgenitor cellsProtein levelsThe 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 ResearchMeSH KeywordsAnimalsBlotting, WesternCalcium-Calmodulin-Dependent Protein Kinase Type 1Calcium-Calmodulin-Dependent Protein KinasesImmunohistochemistryMalePhotic StimulationPrecipitin TestsRatsRats, Sprague-DawleyRetinaSynapsinsModulation of GT-1 DNA-binding activity by calcium-dependent phosphorylation
Maréchal E, Hiratsuka K, Delgado J, Nairn A, Qin J, Chait B, Chua N. Modulation of GT-1 DNA-binding activity by calcium-dependent phosphorylation. Plant Molecular Biology 1999, 40: 373-386. PMID: 10437822, DOI: 10.1023/a:1006131330930.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsArabidopsisBase SequenceBinding SitesCalciumCalcium-Calmodulin-Dependent Protein Kinase Type 2Calcium-Calmodulin-Dependent Protein KinasesDNA PrimersDNA-Binding ProteinsIn Vitro TechniquesMolecular Sequence DataNuclear ProteinsPhosphorylationPlants, ToxicRatsRecombinant ProteinsSequence Homology, Amino AcidSubstrate SpecificityTranscription FactorsConceptsDNA-binding activityCalcium-dependent phosphorylationGene expressionMolecular switchGT-1Analysis of mutantsDNA-binding proteinsLight-grown plantsPost-translational modificationsCalf intestine phosphataseCalcium/calmodulin kinasePhosphorylatable residuesCasein kinaseGene activationMass spectrometry analysisPromoter sequencesDNA bindingKinase activityBoxIICalmodulin kinasePhosphorylationHGT-1Novo synthesisDephosphorylationSpectrometry analysisInhibition 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 inhibitionRegulation of CFTR Cl- ion channels by phosphorylation and dephosphorylation.
Gadsby D, Nairn A. Regulation of CFTR Cl- ion channels by phosphorylation and dephosphorylation. Advances In Second Messenger And Phosphoprotein Research 1999, 33: 79-106. PMID: 10218115, DOI: 10.1016/s1040-7952(99)80006-8.Peer-Reviewed Original ResearchAdenosine TriphosphateBinding SitesCalcium-Calmodulin-Dependent Protein KinasesCyclic AMP-Dependent Protein KinasesCyclic GMP-Dependent Protein KinasesCystic FibrosisCystic Fibrosis Transmembrane Conductance RegulatorHumansIon Channel GatingModels, MolecularPhosphoprotein PhosphatasesPhosphorylationProtein Kinase C
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 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 pancreasRegulation 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
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 proteinsCx43Characterization 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
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 ResearchMeSH KeywordsAnimalsCalciumCalcium ChannelsCalcium-Calmodulin-Dependent Protein Kinase Type 1Calcium-Calmodulin-Dependent Protein KinasesCytoplasmEnzyme ActivationMembrane PotentialsPC12 CellsPhosphorylationRatsConceptsCaM 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 phosphorylationCellsActivationCa2Structural 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-transferase