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
Tumor 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