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 8.5
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
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