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 ResearchConceptsV-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 inhibitorRegulation of Phosphorylation of the GluR1 AMPA Receptor in the Neostriatum by Dopamine and Psychostimulants In Vivo
Snyder G, Allen P, Fienberg A, Valle C, Huganir R, Nairn A, Greengard P. Regulation of Phosphorylation of the GluR1 AMPA Receptor in the Neostriatum by Dopamine and Psychostimulants In Vivo. Journal Of Neuroscience 2000, 20: 4480-4488. PMID: 10844017, PMCID: PMC6772453, DOI: 10.1523/jneurosci.20-12-04480.2000.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBenzazepinesCentral Nervous System StimulantsDopamineDopamine and cAMP-Regulated Phosphoprotein 32In Vitro TechniquesMaleMethamphetamineMiceMice, Inbred C57BLMice, KnockoutMicrowavesNeostriatumNerve Tissue ProteinsOkadaic AcidPhosphoprotein PhosphatasesPhosphoproteinsPhosphorylationProtein Phosphatase 1Protein Phosphatase 2Receptors, AMPAReceptors, Dopamine D1Receptors, Dopamine D2Recombinant Fusion ProteinsSerineConceptsCAMP-dependent protein kinaseProtein phosphatase 2A.AMPA-type glutamate receptorsCalmodulin-dependent kinase IICalcium/calmodulin-dependent kinase IIRegulation of phosphorylationProtein kinase CPhosphatase 2A.Protein kinaseKinase IIPhosphorylation of GluR1Kinase CGluR1 AMPA receptorsPhosphorylationCellular effectorsGlutamate receptorsDARPP-32Physiological activityAMPA receptorsPsychostimulant cocaineChannel conductanceReceptorsD1-type dopamine receptorsActivationVivo
1999
Phosphorylation of the Cytoplasmic Domain of Alzheimer's β-Amyloid Precursor Protein at Ser655 by a Novel Protein Kinase
Isohara T, Horiuchi A, Watanabe T, Ando K, Czernik A, Uno I, Greengard P, Nairn A, Suzuki T. Phosphorylation of the Cytoplasmic Domain of Alzheimer's β-Amyloid Precursor Protein at Ser655 by a Novel Protein Kinase. Biochemical And Biophysical Research Communications 1999, 258: 300-305. PMID: 10329382, DOI: 10.1006/bbrc.1999.0637.Peer-Reviewed Original ResearchConceptsNovel protein kinaseAlzheimer's beta-amyloid precursor proteinProtein kinase CExtracellular signal-regulated kinaseProtein kinaseCytoplasmic domainCalmodulin-dependent protein kinase IIΒ-amyloid precursor proteinPrecursor proteinAlzheimer's β-Amyloid Precursor ProteinSignal-regulated kinaseProtein kinase IIBeta-amyloid precursor proteinKinase IUnidentified proteinsKinase IIKinase CKinaseSer655ProteinAlzheimer's diseaseThr654Rat brainPhosphorylationDomain
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 PDBuCellsInhibitionPhosphorylation 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 proteinsCx43Mutation of the Protein Kinase C Phosphorylation Site on Rat α1 Na+,K+-ATPase Alters Regulation of Intracellular Na+ and pH and Influences Cell Shape and Adhesiveness*
Belusa R, Wang Z, Matsubara T, Sahlgren B, Dulubova I, Nairn A, Ruoslahti E, Greengard P, Aperia A. Mutation of the Protein Kinase C Phosphorylation Site on Rat α1 Na+,K+-ATPase Alters Regulation of Intracellular Na+ and pH and Influences Cell Shape and Adhesiveness*. Journal Of Biological Chemistry 1997, 272: 20179-20184. PMID: 9242694, DOI: 10.1074/jbc.272.32.20179.Peer-Reviewed Original ResearchConceptsProtein kinase CProtein kinase APhosphorylation sitesProtein kinase C phosphorylation sitesKinase C phosphorylation sitesC phosphorylation sitesSites of phosphorylationATPase alpha1Influences cell shapePKC phosphorylation sitesEukaryotic cellsATP hydrolysisPKC phosphorylationRat α1COS cellsCell shapeKinase AWild typeSer-23Kinase CCell adhesionFunctional roleAlters regulationUntransfected cellsPhosphorylationWidespread Neuronal Ectopia Associated with Secondary Defects in Cerebrocortical Chondroitin Sulfate Proteoglycans and Basal Lamina in MARCKS-Deficient Mice
Blackshear P, Silver J, Nairn A, Sulik K, Squier M, Stumpo D, Tuttle J. Widespread Neuronal Ectopia Associated with Secondary Defects in Cerebrocortical Chondroitin Sulfate Proteoglycans and Basal Lamina in MARCKS-Deficient Mice. Experimental Neurology 1997, 145: 46-61. PMID: 9184108, DOI: 10.1006/exnr.1997.6475.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAntibodies, MonoclonalBasement MembraneCerebral CortexChondroitin SulfatesFemaleGene Expression Regulation, DevelopmentalIntracellular Signaling Peptides and ProteinsLamininMaleMembrane ProteinsMiceMice, Mutant StrainsMicroscopy, Electron, ScanningMutationMyristoylated Alanine-Rich C Kinase SubstrateNeurogliaNeuronsPia MaterPregnancyProteinsProteoglycansReticulinSynaptophysinConceptsChondroitin sulfate proteoglycanNeuronal ectopiaBasal laminaSulfate proteoglycanProtein kinase CEmbryonic day 13Basal lamina proteinsReticulin stainingSubarachnoid spaceForebrain commissuresPial membraneDay 13EctopiaGross abnormalitiesRetinal laminationMiceMARCKS deficiencyAbnormalitiesPotential mechanismsNeural substratesMarginal zoneProteolytic destructionKinase CProteoglycansLaminaPhosphorylation of Alzheimer β-Amyloid Precursor-like Proteins †
Suzuki T, Ando K, Isohara T, Oishi M, Lim G, Satoh Y, Wasco W, Tanzi R, Nairn A, Greengard P, Gandy S, Kirino Y. Phosphorylation of Alzheimer β-Amyloid Precursor-like Proteins †. Biochemistry 1997, 36: 4643-4649. PMID: 9109675, DOI: 10.1021/bi962618k.Peer-Reviewed Original ResearchConceptsAlzheimer's beta-amyloid precursor proteinCytoplasmic domain peptidePrecursor-like proteinsProtein kinase CCytoplasmic domainCultured cellsCell cycle-dependent mannerKinase CDomain peptideCycle-dependent mannerAmino acid sequenceHomologous amino acid sequencesGene familyKinase siteAcid sequenceExtracellular domainIntact cellsAPLP2Proteolytic processingAPLP1PhosphorylationPrecursor proteinProteinBeta-amyloid precursor proteinCdc2
1996
Developmental expression of MARCKS and protein kinase C in mice in relation to the exencephaly resulting from MARCKS deficiency
Blackshear P, Lai W, Tuttle J, Stumpo D, Kennington E, Nairn A, Sulik K. Developmental expression of MARCKS and protein kinase C in mice in relation to the exencephaly resulting from MARCKS deficiency. Brain Research 1996, 96: 62-75. PMID: 8922669, DOI: 10.1016/0165-3806(96)00097-1.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBeta-GalactosidaseEmbryonic and Fetal DevelopmentGene Expression Regulation, DevelopmentalGene Expression Regulation, EnzymologicImmunohistochemistryIntracellular Signaling Peptides and ProteinsIsoenzymesMembrane ProteinsMiceMice, Inbred C57BLMice, TransgenicMyristoylated Alanine-Rich C Kinase SubstrateNerve Tissue ProteinsNeural Tube DefectsPhosphorylationProtein Kinase CProteinsRecombinant Fusion ProteinsConceptsProtein kinase CNeural tube closureKinase CPlasma membraneTube closureNeural tubeCranial neural tube closureMajor cellular substrateEmbryonic day 8.5MARCKS deficiencySpecific cell typesE8.5 embryosCranial neural tubeMouse geneFunctional defectsMARCKS proteinPerinatal lethalityMARCKSCellular substratesCranial neurulationMARCKS expressionUnderlying mesenchymeDevelopmental expressionPKC-alphaDay 8.5Amyloid 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 substrate
1994
Specificity of protein kinase inhibitor peptides and induction of long-term potentiation.
Hvalby O, Hemmings H, Paulsen O, Czernik A, Nairn A, Godfraind J, Jensen V, Raastad M, Storm J, Andersen P. Specificity of protein kinase inhibitor peptides and induction of long-term potentiation. Proceedings Of The National Academy Of Sciences Of The United States Of America 1994, 91: 4761-4765. PMID: 8197132, PMCID: PMC43868, DOI: 10.1073/pnas.91.11.4761.Peer-Reviewed Original ResearchConceptsProtein kinase CProtein kinase inhibitor peptideProtein kinase inhibitionInhibitor peptideDependent protein kinase IIInhibition of PKCKinase inhibitionProtein kinase IIPseudosubstrate domainAutoregulatory domainProtein kinasePhysiological assaysKinase IIKinase CLong-term potentiationSynthetic peptide analoguesInductionPeptide analoguesHippocampal neuronsPeptidesIntracellular deliveryBlockade of inductionInduction of LTPInhibitionVitroCorrelation 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
1993
Protein Phosphorylation Regulates Relative Utilization of Processing Pathways for Alzheimer β/A4 Amyloid Precursor Proteina
GANDY S, CAPORASO G, BUXBAUM J, DA CRUZ E SILVA O, IVERFELDT K, NORDSTEDT C, SUZUKI T, CZERNIK A, NAIRN A, GREENGARD P. Protein Phosphorylation Regulates Relative Utilization of Processing Pathways for Alzheimer β/A4 Amyloid Precursor Proteina. Annals Of The New York Academy Of Sciences 1993, 695: 117-121. PMID: 8239268, DOI: 10.1111/j.1749-6632.1993.tb23038.x.Peer-Reviewed Original ResearchConceptsOkadaic acid-sensitive proteinAlzheimer amyloid precursor proteinAcid-sensitive proteinProtein kinase CProtein phosphorylationKinase CCalmodulin-dependent protein kinase IICalcium/calmodulin-dependent protein kinase IIProtein kinase IISignal transductionPhosphorylation stateModulation of betaKinase IISecretory cleavageSubstrate redistributionPrecursor proteinCurrent experimental evidenceAmyloid precursor proteinProteinCleavage pathwayPhosphorylationProcessing pathwaysSubstrate activationSer655APP metabolism
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 morphologyProteinPhosphorylationActinMembraneCytoskeletonCalmodulinCytoplasmBindsCharacterization of the cystic fibrosis transmembrane conductance regulator in a colonocyte cell line.
Cohn J, Nairn A, Marino C, Melhus O, Kole J. Characterization of the cystic fibrosis transmembrane conductance regulator in a colonocyte cell line. Proceedings Of The National Academy Of Sciences Of The United States Of America 1992, 89: 2340-2344. PMID: 1372442, PMCID: PMC48653, DOI: 10.1073/pnas.89.6.2340.Peer-Reviewed Original ResearchConceptsCystic fibrosis transmembrane conductance regulatorFibrosis transmembrane conductance regulatorTransmembrane conductance regulatorConductance regulatorTwo-dimensional phosphopeptide mappingT84 cellsProtein kinase ACell linesProtein kinase CSDS/PAGEPhosphopeptide mappingPhosphorylation sitesProminent substrateCFTR peptidesEquivalent proteinsKinase ASame proteinKinase CTerminal sequenceCell lysatesN-glycanaseProteinAnti-peptide antibodiesImmunoblot signalsCFTR immunoreactivity
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 IIRegulation 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 SubstrateN-Formylmethionine Leucyl-PhenylalanineNeutrophilsOkadaic 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 filopodiaFilopodiaPhosphorylation of connexin 32, a hepatocyte gap‐junction protein, by cAMP‐dependent protein kinase, protein kinase C and Ca2+/calmodulin‐dependent protein kinase II
SAEZ J, NAIRN A, CZERNIK A, SPRAY D, HERTZBERG E, GREENGARD P, BENNETT M. Phosphorylation of connexin 32, a hepatocyte gap‐junction protein, by cAMP‐dependent protein kinase, protein kinase C and Ca2+/calmodulin‐dependent protein kinase II. The FEBS Journal 1990, 192: 263-273. PMID: 2170122, DOI: 10.1111/j.1432-1033.1990.tb19223.x.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsCalcium-Calmodulin-Dependent Protein KinasesConnexinsElectrophoresis, Gel, Two-DimensionalElectrophoresis, Polyacrylamide GelFemaleLiverMembrane ProteinsMolecular Sequence DataPeptide FragmentsPeptidesPhosphopeptidesPhosphorylationProtein Kinase CProtein KinasesRatsRats, Inbred StrainsConceptsProtein kinase CCAMP-dependent protein kinaseDependent protein kinase IIGap junction proteinPhosphopeptide mappingProtein kinaseSeryl residuesProtein kinase IICAMP-PKKinase IIKinase CCell typesConnexin 32PK IIPhosphoamino acid analysisDifferent gap junction proteinsSites of phosphorylationPhosphorylated synthetic peptideCAMP-PK activityGap junctionsAmino acid sequencingActivation of PKCDifferent cell typesPhysiological substratesSynthetic peptidesTumor necrosis factor alpha modifies agonist-dependent responses in human neutrophils by inducing the synthesis and myristoylation of a specific protein kinase C substrate.
Thelen M, Rosen A, Nairn A, Aderem A. Tumor necrosis factor alpha modifies agonist-dependent responses in human neutrophils by inducing the synthesis and myristoylation of a specific protein kinase C substrate. Proceedings Of The National Academy Of Sciences Of The United States Of America 1990, 87: 5603-5607. PMID: 2116001, PMCID: PMC54375, DOI: 10.1073/pnas.87.15.5603.Peer-Reviewed Original ResearchMeSH KeywordsColony-Stimulating FactorsGranulocyte-Macrophage Colony-Stimulating FactorGrowth SubstancesHumansIn Vitro TechniquesInterferon-gammaIntracellular Signaling Peptides and ProteinsKineticsLipopolysaccharidesLysineMembrane ProteinsMyristic AcidMyristic AcidsMyristoylated Alanine-Rich C Kinase SubstrateNeutrophilsPhosphatesPhosphopeptidesPhosphorylationProtein BiosynthesisProtein Kinase CProteinsRecombinant ProteinsTumor Necrosis Factor-alphaConceptsSpecific protein kinase C substrateProtein kinase C substrateProtein kinase CC substrateKinase C.Kinase CAlanine-rich C kinase substratePhosphorylation of MARCKSN-terminal glycineC kinase substrateProtein kinase C.Agonist-dependent responsesIdentical phosphopeptidesKinase substrateTransduction pathwaysMARCKS phosphorylationMARCKSEnhanced phosphorylationHuman neutrophilsMurine fibroblastsEffector moleculesProteinPhosphorylationMyristoylationBovine brain