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 form
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 ResearchConceptsProtein 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 substrateStructure, 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
1993
Purification and characterization of calmodulin-dependent protein kinase III from rabbit reticulocytes and rat pancreas
Mitsui K, Brady M, Palfrey H, Nairn A. Purification and characterization of calmodulin-dependent protein kinase III from rabbit reticulocytes and rat pancreas. Journal Of Biological Chemistry 1993, 268: 13422-13433. PMID: 8514778, DOI: 10.1016/s0021-9258(19)38667-3.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsCalcium-Calmodulin-Dependent Protein KinasesCalmodulinCattleChromatography, GelElectrophoresis, Polyacrylamide GelElongation Factor 2 KinaseHeat-Shock ProteinsMolecular Sequence DataPancreasPeptide Elongation Factor 2Peptide Elongation FactorsPeptide MappingPhosphoproteinsPhosphorylationProtein KinasesRabbitsRatsReticulocytesSubstrate SpecificityConceptsEukaryotic elongation factor 2CaM kinase IIICalmodulin-dependent protein kinase IIIProtein kinase IIIKinase IIIProtein kinaseRabbit reticulocytesCAMP-dependent protein kinaseYeast EF-2Heat shock protein Hsp90Novel protein kinaseElongation factor 2Amino acid sequencingPhosphopeptide mappingSodium dodecyl sulfate-polyacrylamide gel electrophoresisDodecyl sulfate-polyacrylamide gel electrophoresisProtein Hsp90Catalytic subunitSulfate-polyacrylamide gel electrophoresisSeryl residuesMajor polypeptidesSubstrate ATPHsp90Factor 2Gel electrophoresisPhosphorylation of elongation factor 2 in normal and malignant rat glial cells.
Bagaglio DM, Cheng EH, Gorelick FS, Mitsui K, Nairn AC, Hait WN. Phosphorylation of elongation factor 2 in normal and malignant rat glial cells. Cancer Research 1993, 53: 2260-4. PMID: 8485712.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCalciumCalcium-Calmodulin-Dependent Protein KinasesCalmodulinCell DivisionCells, CulturedElongation Factor 2 KinaseGliomaMaleNeurogliaPeptide Elongation Factor 2Peptide Elongation FactorsPhosphorylationPrecipitin TestsProtein KinasesRatsRats, Sprague-DawleyTrifluoperazineTumor Cells, CulturedConceptsRat brain white matterNormal glial tissueGlial tissueGlioma cellsC6 cellsC6 rat glioma cellsCaM kinase IIIRat glial cellsFactor 2Rat glioma cellsBrain white matterNormal gliaElongation factor 2Glial cellsRat brainWhite matterTumor tissueBasal levelsIII activityCellular proliferationTissueDependent proteinsCellsEndogenous substratesHomogenates
1992
MARCKS is an actin filament crosslinking protein regulated by protein kinase C and calcium–calmodulin
Hartwig J, Thelen M, Resen A, Janmey P, Nairn A, Aderem A. MARCKS is an actin filament crosslinking protein regulated by protein kinase C and calcium–calmodulin. Nature 1992, 356: 618-622. PMID: 1560845, DOI: 10.1038/356618a0.Peer-Reviewed Original ResearchMeSH KeywordsActin CytoskeletonActinsAmino Acid SequenceAnimalsBrainCalciumCalmodulinCattleCross-Linking ReagentsHomeostasisIntracellular Signaling Peptides and ProteinsKineticsMembrane ProteinsMicroscopy, ElectronMolecular Sequence DataMusclesMyristoylated Alanine-Rich C Kinase SubstratePhosphorylationProtein Kinase CProteinsRabbitsTime FactorsConceptsProtein kinase CPlasma membraneCalcium-calmodulinKinase CSignal transduction pathwaysPKC signal transduction pathwayActin filament crosslinking proteinActin cytoskeletonActin assemblyTransduction pathwaysMARCKS proteinFilamentous actinCrosslinking activitySpecific substratesSubstrates bindMARCKSCell morphologyProteinPhosphorylationActinMembraneCytoskeletonCalmodulinCytoplasmBindsCalmodulin and Protein Kinase C Cross‐Talk: The MARCKS Protein is an Actin Filament and Plasma Membrane Cross‐Linking Protein Regulated by Protein Kinase C Phosphorylation and by Calmodulin
Nairn A, Aderem A. Calmodulin and Protein Kinase C Cross‐Talk: The MARCKS Protein is an Actin Filament and Plasma Membrane Cross‐Linking Protein Regulated by Protein Kinase C Phosphorylation and by Calmodulin. Novartis Foundation Symposia 1992, 164: 145-161. PMID: 1395931, DOI: 10.1002/9780470514207.ch10.Peer-Reviewed Original ResearchConceptsCross-linking proteinsPlasma membraneF-actin cross-linking proteinsActin filamentsProtein kinase C phosphorylationAlanine-rich C kinase substrateKinase C phosphorylationGrowth factor-dependent mitogenesisSignal transduction pathwaysC kinase substrateActin-binding propertiesKinase substrateActivation of PKCTransduction pathwaysC phosphorylationMARCKS proteinInhibits phosphorylationMARCKSMembrane interactionsCycles of releaseSpecific substratesPhosphorylationPKCProteinCalmodulin
1990
Role 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
1987
Identification of the major Mr 100,000 substrate for calmodulin-dependent protein kinase III in mammalian cells as elongation factor-2.
Nairn A, Palfrey H. Identification of the major Mr 100,000 substrate for calmodulin-dependent protein kinase III in mammalian cells as elongation factor-2. Journal Of Biological Chemistry 1987, 262: 17299-17303. PMID: 3693353, DOI: 10.1016/s0021-9258(18)45377-x.Peer-Reviewed Original ResearchConceptsProtein kinase IIIElongation factor 2Kinase IIIMammalian cellsThreonine residuesCalmodulin-dependent protein kinase IIIDependent protein kinase IIIPhosphorylated EF-2Endogenous GTPase activityAmino acid sequencingSpecies of MrFactor 2Inhibits protein synthesisTryptic phosphopeptidesGTPase activityNucleic acid sequencingCytoplasmic localizationMajor substrateN-terminalPeptidyl-tRNATerminal sequenceSalt-washed ribosomesProtein synthesisEF-1Thr-AspCa2+/calmodulin-dependent protein kinase II: identification of autophosphorylation sites responsible for generation of Ca2+/calmodulin-independence.
Lai Y, Nairn AC, Gorelick F, Greengard P. Ca2+/calmodulin-dependent protein kinase II: identification of autophosphorylation sites responsible for generation of Ca2+/calmodulin-independence. Proceedings Of The National Academy Of Sciences Of The United States Of America 1987, 84: 5710-5714. PMID: 3475699, PMCID: PMC298932, DOI: 10.1073/pnas.84.16.5710.Peer-Reviewed Original Research
1984
The amino acid sequence of rabbit skeletal muscle calmodulin
Nairn A, Grand R, Perry S. The amino acid sequence of rabbit skeletal muscle calmodulin. FEBS Letters 1984, 167: 215-220. PMID: 6698209, DOI: 10.1016/0014-5793(84)80129-5.Peer-Reviewed Original ResearchConceptsSingle polypeptide chainMyosin light chain kinaseBlocked N terminusRabbit skeletal muscleLight chain kinasePhosphorylase kinaseMammalian calmodulinN-terminusPolypeptide chainResidues 48Chain kinaseAmide assignmentsCalmodulinLow ionic strength bufferKinaseSkeletal muscleIonic strength bufferSequenceN-terminal tripeptideStrength bufferTerminal tripeptideTerminusSubunitsProteinResidues
1980
THE RELATIONSHIP OF THE STRUCTURE TO THE FUNCTION OF CALMODULIN IN THE MYOSIN LIGHT CHAIN KINASE SYSTEM
Nairn A, Grand R, Wall C, Perry S. THE RELATIONSHIP OF THE STRUCTURE TO THE FUNCTION OF CALMODULIN IN THE MYOSIN LIGHT CHAIN KINASE SYSTEM. Annals Of The New York Academy Of Sciences 1980, 356: 413-414. PMID: 6940506, DOI: 10.1111/j.1749-6632.1980.tb29653.x.Peer-Reviewed Original ResearchThe 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
The Role of Calmodulin in the Structure and Regulation of Phosphorylase Kinase from Rabbit Skeletal Muscle
SHENOLIKAR S, COHEN P, COHEN P, NAIRN A, PERRY S. The Role of Calmodulin in the Structure and Regulation of Phosphorylase Kinase from Rabbit Skeletal Muscle. The FEBS Journal 1979, 100: 329-337. PMID: 159817, DOI: 10.1111/j.1432-1033.1979.tb04175.x.Peer-Reviewed Original ResearchThe role of calmodulin in the myosin light-chain kinase system [proceedings].
NAIRN A, PERRY S. The role of calmodulin in the myosin light-chain kinase system [proceedings]. Biochemical Society Transactions 1979, 7: 966-7. PMID: 229046, DOI: 10.1042/bst0070966.Peer-Reviewed Original ResearchCalmodulin 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