1995
Isotype-specific Activation of Cystic Fibrosis Transmembrane Conductance Regulator-Chloride Channels by cGMP-dependent Protein Kinase II (∗)
French P, Bijman J, Edixhoven M, Vaandrager A, Scholte B, Lohmann S, Nairn A, de Jonge H. Isotype-specific Activation of Cystic Fibrosis Transmembrane Conductance Regulator-Chloride Channels by cGMP-dependent Protein Kinase II (∗). Journal Of Biological Chemistry 1995, 270: 26626-26631. PMID: 7592887, DOI: 10.1074/jbc.270.44.26626.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAnimalsCattleCell LineCell MembraneChloride ChannelsCyclic GMP-Dependent Protein KinasesCystic Fibrosis Transmembrane Conductance RegulatorEnzyme InhibitorsIntestinesIsoenzymesKineticsLungMacromolecular SubstancesMarine ToxinsMembrane PotentialsMicrovilliOxazolesPeptide FragmentsPhosphopeptidesPhosphorylationProtein Phosphatase 1Protein Tyrosine PhosphatasesRatsRecombinant ProteinsSwineTransfectionConceptsProtein kinaseType II cGMP-dependent protein kinaseCGMP-dependent protein kinase IICAMP-dependent protein kinaseCystic fibrosis transmembrane conductance regulator (CFTR) chloride channelCGMP-dependent protein kinaseCystic fibrosis transmembrane conductance regulatorFibrosis transmembrane conductance regulatorTransmembrane conductance regulatorProtein kinase IINIH 3T3 fibroblastsRat intestinal cell lineRecombinant CFTRCF 2Presence of cGMPProtein phosphatasePresence of ATPCAK activationPhosphatase 1Phosphopeptide mapsCatalytic subunitCalyculin ACatalytic fragmentKinase IIConductance regulator
1994
Subcellular localization of CFTR to endosomes in a ductal epithelium
Webster P, Vanacore L, Nairn A, Marino C. Subcellular localization of CFTR to endosomes in a ductal epithelium. American Journal Of Physiology 1994, 267: c340-c348. PMID: 7521124, DOI: 10.1152/ajpcell.1994.267.2.c340.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCell MembraneCystic FibrosisCystic Fibrosis Transmembrane Conductance RegulatorEndocytosisEpitheliumFluorescent Antibody TechniqueImmunohistochemistryMaleMembrane ProteinsMicroscopy, FluorescenceOrganellesRatsRats, Sprague-DawleyReceptors, Cell SurfaceSubcellular FractionsSubmandibular GlandTissue DistributionConceptsCystic fibrosis transmembrane conductance regulatorPlasma membraneFibrosis transmembrane conductance regulatorApical plasma membraneAnti-CFTR antibodiesNormal epithelial cell populationsTransmembrane conductance regulatorCytochemical evidenceReceptor-mediated endocytosisCFTR moleculesEpithelial cell populationsCellular processesSubcellular compartmentsSubcellular localizationEarly endosomesMembrane recyclingConductance regulatorSubcellular distributionSubapical vesiclesApical poleEndosomesCFTR functionImmunoelectron microscopyCell populationsCFTR immunoreactivity
1992
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
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
Identification and localization of a dogfish homolog of human cystic fibrosis transmembrane conductance regulator.
Marshall J, Martin K, Picciotto M, Hockfield S, Nairn A, Kaczmarek L. Identification and localization of a dogfish homolog of human cystic fibrosis transmembrane conductance regulator. Journal Of Biological Chemistry 1991, 266: 22749-22754. PMID: 1718999, DOI: 10.1016/s0021-9258(18)54631-7.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBase SequenceCell MembraneCloning, MolecularCystic FibrosisCystic Fibrosis Transmembrane Conductance RegulatorDNADogfishHumansImmunoenzyme TechniquesMembrane ProteinsMolecular Sequence DataMolecular WeightProtein KinasesRectumSebaceous GlandsSequence Homology, Nucleic AcidSubstrate SpecificityConceptsCystic fibrosis transmembrane conductance regulatorHuman cystic fibrosis transmembrane conductance regulatorFibrosis transmembrane conductance regulatorTransmembrane conductance regulatorDogfish proteinRectal glandConductance regulatorPutative substrate sitesCyclic AMP-dependent protein kinaseAMP-dependent protein kinaseMajor phosphorylation siteCyclic AMP-dependent protein phosphorylationApical plasma membraneAmino acid sequenceStudy of regulationPhosphorylation sitesProtein phosphorylationCDNA clonesProtein kinaseSimilar molecular massCFTR sequencePlasma membraneAcid sequenceImmunolocalization studiesMolecular massRegulation 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