2022
Myosin light chain phosphatase catalytic subunit dephosphorylates cardiac myosin via mechanisms dependent and independent of the MYPT regulatory subunits
Lee E, Liu Z, Nguyen N, Nairn A, Chang AN. Myosin light chain phosphatase catalytic subunit dephosphorylates cardiac myosin via mechanisms dependent and independent of the MYPT regulatory subunits. Journal Of Biological Chemistry 2022, 298: 102296. PMID: 35872014, PMCID: PMC9418503, DOI: 10.1016/j.jbc.2022.102296.Peer-Reviewed Original ResearchConceptsMyosin light chain phosphataseRegulatory light chainRegulatory subunitCatalytic subunitPhosphatase catalytic subunitMain catalytic subunitSmooth muscle myosin light chain phosphataseNon-muscle cellsMuscle myosin light chain phosphataseMyosin regulatory light chainMyosin light chain kinaseLight chain kinasePP1cβTrimeric proteinConditional knockout miceLight chain phosphatasePhosphatase activitySubunitsPhosphate/Chain kinaseMuscle pathogenesisPhysiological regulationKnockout animalsMain isoformsProtein
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 brainCalcium/calmodulin-dependent protein kinase II increases glutamate and noradrenaline release from synaptosomes
Nichols R, Sihra T, Czernik A, Nairn A, Greengard P. Calcium/calmodulin-dependent protein kinase II increases glutamate and noradrenaline release from synaptosomes. Nature 1990, 343: 647-651. PMID: 2154695, DOI: 10.1038/343647a0.Peer-Reviewed Original ResearchConceptsNeurotransmitter releaseRat brain synaptosomesSquid giant synapseRelease of neurotransmittersNoradrenaline releaseGlutamate releaseNerve terminalsBrain synaptosomesNervous systemUnidentified neurotransmitterGiant synapseDependent protein kinase IIVertebrate nervous systemRats calciumProtein kinase IINeurotransmittersInduced releasePK IISynaptosomesCalcium-dependent protein phosphorylationGlutamateKinase IIReleaseNoradrenalineInitial rate