2000
Severed Channels Probe Regulation of Gating of Cystic Fibrosis Transmembrane Conductance Regulator by Its Cytoplasmic Domains
Csanády L, Chan K, Seto-Young D, Kopsco D, Nairn A, Gadsby D. Severed Channels Probe Regulation of Gating of Cystic Fibrosis Transmembrane Conductance Regulator by Its Cytoplasmic Domains. The Journal Of General Physiology 2000, 116: 477-500. PMID: 10962022, PMCID: PMC2233695, DOI: 10.1085/jgp.116.3.477.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAdenylyl ImidodiphosphateAnimalsBase SequenceCyclic AMP-Dependent Protein KinasesCystic FibrosisCystic Fibrosis Transmembrane Conductance RegulatorDNA PrimersFemaleHumansIn Vitro TechniquesIon Channel GatingModels, BiologicalMutationOocytesPhosphorylationProtein Structure, TertiaryRecombinant ProteinsXenopusConceptsR domainCFTR channelsPhosphorylated R domainWild-type CFTR channelsCytoplasmic regulatory domainCystic fibrosis transmembrane conductance regulatorNucleotide Binding DomainFibrosis transmembrane conductance regulatorDetailed functional characteristicsWT channelsApparent ATP affinityTransmembrane conductance regulatorCFTR Cl- channelPresence of PKANonhydrolyzable ATP analogue AMPPNPATP analogue AMPPNPATP bindingRegulatory domainCytoplasmic domainWt-CFTRBinding domainsGating eventsConductance regulatorATP affinityFunctional interactionSevered Molecules Functionally Define the Boundaries of the Cystic Fibrosis Transmembrane Conductance Regulator's Nh2-Terminal Nucleotide Binding Domain
Chan K, Csanády L, Seto-Young D, Nairn A, Gadsby D. Severed Molecules Functionally Define the Boundaries of the Cystic Fibrosis Transmembrane Conductance Regulator's Nh2-Terminal Nucleotide Binding Domain. The Journal Of General Physiology 2000, 116: 163-180. PMID: 10919864, PMCID: PMC2229491, DOI: 10.1085/jgp.116.2.163.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine MonophosphateAnimalsCystic Fibrosis Transmembrane Conductance RegulatorEndoplasmic ReticulumEpitopesFemaleGene DeletionGene ExpressionIon Channel GatingKineticsMembrane PotentialsMolecular Sequence DataMutagenesisOligopeptidesOocytesPatch-Clamp TechniquesPeptide FragmentsPeptidesPrecipitin TestsProtein BindingProtein Structure, TertiarySequence Homology, Amino AcidTransfectionXenopus laevisConceptsR domainCFTR channelsCOOH terminusMature formFull-length CFTRCystic fibrosis transmembrane conductance regulatorAmino acids 590Nucleotide Binding DomainFibrosis transmembrane conductance regulatorExcised patch recordingsChannel activityFamily of ATPRequirement of phosphorylationCFTR channel activityTransmembrane conductance regulatorNBD1 domainSmaller single-channel conductanceCFTR polypeptideTransmembrane domainATP bindingRegulatory domainCassette proteinNBD structuresNBD1Binding domains
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 regulatorCystic Fibrosis Transmembrane Conductance Regulator Is Found Within Brain Ventricular Epithelium and Choroid Plexus
Hincke M, Nairn A, Staines W. Cystic Fibrosis Transmembrane Conductance Regulator Is Found Within Brain Ventricular Epithelium and Choroid Plexus. Journal Of Neurochemistry 1995, 64: 1662-1668. PMID: 7534334, DOI: 10.1046/j.1471-4159.1995.64041662.x.Peer-Reviewed Original ResearchConceptsCystic fibrosis transmembrane conductance regulatorFibrosis transmembrane conductance regulatorTransmembrane conductance regulatorConductance regulatorCystic fibrosis gene productBrain Ventricular EpitheliumCyclic AMP-dependent phosphorylationGene productsCFTR proteinFine punctaChloride transportersCl- channelsCyclic AMP-elevating agentsEpendymal functionWestern blottingRegulatorVentricular epitheliumPhosphorylationChoroid plexusProteinTransportersRodent brainPunctaRegulationMicrodissectionCaMKI CaM-dependent protein kinase I (vertebrates)
Edelman A, Nairn A. CaMKI CaM-dependent protein kinase I (vertebrates). 1995, 128-130. DOI: 10.1016/b978-012324719-3/50029-7.Peer-Reviewed Original ResearchCystic fibrosis transmembrane conductance regulatorKinase IProtein kinase ICaM kinase ICAMP response element-binding proteinCaM-dependent protein kinase ICalmodulin-dependent protein kinase IPartial amino acid sequence dataShort N-terminal extensionLong C-terminal extensionAmino acid sequence dataFibrosis transmembrane conductance regulatorN-terminal extensionC-terminal extensionCaM-binding domainSynaptic vesicle functionAmino acid sequenceBrain cDNA libraryRat brain cDNA libraryTransmembrane conductance regulatorWidespread tissue distributionResponse element-binding proteinElement-binding proteinIon channel activityKinase domain
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 immunoreactivityCoupling of CFTR Cl− channel gating to an ATP hydrolysis cycle
Baukrowitz T, Hwang T, Nairn A, Gadsby D. Coupling of CFTR Cl− channel gating to an ATP hydrolysis cycle. Neuron 1994, 12: 473-482. PMID: 7512348, DOI: 10.1016/0896-6273(94)90206-2.Peer-Reviewed Original ResearchConceptsCystic fibrosis transmembrane conductance regulatorATP hydrolysis cycleHydrolysis cycleCFTR channelsFibrosis transmembrane conductance regulatorProtein kinase ATransmembrane conductance regulatorATP hydrolysisKinase AConductance regulatorNucleoside triphosphatesChannel openingInorganic phosphate analogueATPPhosphate analogueCardiac myocytesInorganic phosphateMean open timeRegulatorHydrolysis productsBeF3Open timeCycleTriphosphate
1992
The protein kinase A-regulated cardiac CI− channel resembles the cystic fibrosis transmembrane conductance regulator
Nagel G, Hwang T, Nastiuk K, Nairn A, Gadsbyt D. The protein kinase A-regulated cardiac CI− channel resembles the cystic fibrosis transmembrane conductance regulator. Nature 1992, 360: 81-84. PMID: 1279437, DOI: 10.1038/360081a0.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAnimalsBiological Transport, ActiveBlotting, NorthernChloride ChannelsChlorineCystic Fibrosis Transmembrane Conductance RegulatorGuanosine TriphosphateGuinea PigsIn Vitro TechniquesIon Channel GatingMembrane PotentialsMembrane ProteinsMyocardiumPhosphorylationProtein KinasesReceptors, Adrenergic, betaRNAConceptsCystic fibrosis transmembrane conductance regulatorFibrosis transmembrane conductance regulatorTransmembrane conductance regulatorConductance regulatorCyclic AMP-dependent protein kinaseAMP-dependent protein kinasePKA catalytic subunitResult of phosphorylationPhosphorylated channelsCatalytic subunitProtein kinaseSingle-channel conductanceNucleoside triphosphatesPhosphorylationMembrane potentialEpithelial cellsChannel activationRegulatorChannel conductanceCystic fibrosisKinaseCardiac ventricular myocytesSubunitsProteinUnitary current amplitudeCharacterization of the cystic fibrosis transmembrane conductance regulator in a colonocyte cell line.
Cohn J, Nairn A, Marino C, Melhus O, Kole J. Characterization of the cystic fibrosis transmembrane conductance regulator in a colonocyte cell line. Proceedings Of The National Academy Of Sciences Of The United States Of America 1992, 89: 2340-2344. PMID: 1372442, PMCID: PMC48653, DOI: 10.1073/pnas.89.6.2340.Peer-Reviewed Original ResearchConceptsCystic fibrosis transmembrane conductance regulatorFibrosis transmembrane conductance regulatorTransmembrane conductance regulatorConductance regulatorTwo-dimensional phosphopeptide mappingT84 cellsProtein kinase ACell linesProtein kinase CSDS/PAGEPhosphopeptide mappingPhosphorylation sitesProminent substrateCFTR peptidesEquivalent proteinsKinase ASame proteinKinase CTerminal sequenceCell lysatesN-glycanaseProteinAnti-peptide antibodiesImmunoblot signalsCFTR immunoreactivity
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 mass