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
1988
Skeletal muscle sarcolemma proteins as targets for adenosine 3′:5′-monophosphate-dependent and calcium-dependent protein kinases
Walaas S, Horn R, Nairn A, Walaas O, Adler A. Skeletal muscle sarcolemma proteins as targets for adenosine 3′:5′-monophosphate-dependent and calcium-dependent protein kinases. Archives Of Biochemistry And Biophysics 1988, 262: 245-258. PMID: 3355169, DOI: 10.1016/0003-9861(88)90186-5.Peer-Reviewed Original ResearchConceptsCalcium-dependent protein kinaseProtein kinaseProtein phosphorylationPhosphorylation systemRat skeletal muscle plasma membranesCGMP-dependent protein kinaseIntrinsic membrane proteinsProtein phosphorylation systemsSkeletal muscle cellsSkeletal muscle plasma membranesSarcolemma proteinsMembrane proteinsProtein speciesMuscle plasma membranePlasma membraneMembrane targetsSpecific substratesKinaseMultiple hormonesDistinct setsProteinPhosphoproteinMuscle cellsPhosphorylationReticulum fractions
1982
Serum antibodies that distinguish between the phospho- and dephospho-forms of a phosphoprotein
Nairn A, Detre J, Casnellie J, Greengard P. Serum antibodies that distinguish between the phospho- and dephospho-forms of a phosphoprotein. Nature 1982, 299: 734-736. PMID: 6289133, DOI: 10.1038/299734a0.Peer-Reviewed Original Research