1997
Phosphorylation 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 proteinsCx43
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 filopodiaFilopodia
1989
Regulation of Chloride Channels by Protein Kinase C in Normal and Cystic Fibrosis Airway Epithelia
Li M, McCann J, Anderson M, Clancy J, Liedtke C, Nairn A, Greengard P, Welsch M. Regulation of Chloride Channels by Protein Kinase C in Normal and Cystic Fibrosis Airway Epithelia. Science 1989, 244: 1353-1356. PMID: 2472006, DOI: 10.1126/science.2472006.Peer-Reviewed Original ResearchConceptsProtein kinase CChloride channelsKinase CApical membrane chloride channelMembrane chloride channelCystic fibrosis cellsMembrane proteinsCell-free membraneCystic fibrosis airway epitheliaChloride secretionIntact cellsPhorbol esterPhysiological statusDefective regulationAirway epithelial cellsEpithelial cellsCellsRegulationChannel inactivationCystic fibrosisActivationCalcium concentrationLow calcium concentrationsProteinAirway epithelium