1999
The Second Hydrophobic Domain Contributes to the Kinetic Properties of Epithelial Sodium Channels*
Fyfe G, Zhang P, Canessa C. The Second Hydrophobic Domain Contributes to the Kinetic Properties of Epithelial Sodium Channels*. Journal Of Biological Chemistry 1999, 274: 36415-36421. PMID: 10593937, DOI: 10.1074/jbc.274.51.36415.Peer-Reviewed Original ResearchConceptsSecond hydrophobic domainEpithelial sodium channelBeta subunitHydrophobic domainWild-type subunitsSecond transmembrane domainENaC/Deg familyTransmembrane domainChimeric subunitsSodium channelsFunctional poresSubunit alphaAlpha subunitKinetic propertiesFunctional channelsSubunitsSingle-channel conductanceIon channelsSpecific sequencesXenopus oocytesSmall conductanceOpen probabilityChannel conductanceFunctional propertiesAmiloride affinityThe Serum and Glucocorticoid Kinase sgk Increases the Abundance of Epithelial Sodium Channels in the Plasma Membrane of Xenopus Oocytes*
de la Rosa D, Zhang P, Náray-Fejes-Tóth A, Fejes-Tóth G, Canessa C. The Serum and Glucocorticoid Kinase sgk Increases the Abundance of Epithelial Sodium Channels in the Plasma Membrane of Xenopus Oocytes*. Journal Of Biological Chemistry 1999, 274: 37834-37839. PMID: 10608847, DOI: 10.1074/jbc.274.53.37834.Peer-Reviewed Original ResearchConceptsCarboxyl terminusPlasma membraneEpithelial sodium channelSerine/threonineXenopus oocytesNumber of ENaCsGlucocorticoid-induced kinaseRenal epithelial cellsThreonine kinaseSodium channelsMembrane abundanceTyrosine residuesGamma subunitsSGKAbundance of ENaCCell surfacePhosphorylationTerminusAmiloride-sensitive sodium transportAbundanceSodium transportKinaseENaC.Epithelial cellsSubunits
1998
In vivo phosphorylation of the epithelial sodium channel
Shimkets R, Lifton R, Canessa C. In vivo phosphorylation of the epithelial sodium channel. Proceedings Of The National Academy Of Sciences Of The United States Of America 1998, 95: 3301-3305. PMID: 9501257, PMCID: PMC19736, DOI: 10.1073/pnas.95.6.3301.Peer-Reviewed Original ResearchMeSH KeywordsAldosteroneAmilorideAmino Acid SequenceAnimalsColforsinCyclic AMP-Dependent Protein KinasesDogsEpithelial CellsEpithelial Sodium ChannelsInsulinMolecular Sequence DataNephronsPeptide MappingPhosphopeptidesPhosphorylationProtein Kinase CRatsSodium Channel AgonistsSodium ChannelsTransfectionConceptsCarboxyl terminusEpithelial sodium channelAlpha subunitGamma subunitsDe novo phosphorylationSubunit of ENaC.Stable cotransfectionVivo phosphorylationProtein kinaseEpithelial cell lineSodium channelsMolecular mechanismsActivity of ENaCPhosphorylationSubunitsCell linesTerminusProteinBetaKinaseCotransfectionBasal stateSerineThreonineENaC.
1995
Cloning of a bovine renal epithelial Na+ channel subunit
Fuller C, Awayda M, Arrate M, Bradford A, Morris R, Canessa C, Rossier B, Benos D. Cloning of a bovine renal epithelial Na+ channel subunit. American Journal Of Physiology 1995, 269: c641-c654. PMID: 7573394, DOI: 10.1152/ajpcell.1995.269.3.c641.Peer-Reviewed Original ResearchConceptsChannel subunitsOpen reading frameProtein kinase A.Gamma-ENaC subunitsCDNA expression libraryProtein kinase CVitro translationCDNA clonesBovine cDNAXenopus laevis oocytesPancreatic microsomesAcid proteinReading frameNovel isoformBovine homologueExpression libraryConsensus sequenceKinase CBase pairsAlpha-hENaCXenopus oocytesChimeric channelsHuman counterpartLaevis oocytesSubunits
1994
Membrane topology of the epithelial sodium channel in intact cells
Canessa C, Merillat A, Rossier B. Membrane topology of the epithelial sodium channel in intact cells. American Journal Of Physiology 1994, 267: c1682-c1690. PMID: 7810611, DOI: 10.1152/ajpcell.1994.267.6.c1682.Peer-Reviewed Original ResearchConceptsLarge hydrophilic loopHydrophilic loopIntact cellsMembrane topologyEpithelial sodium channelPutative transmembrane domainsStop-transfer signalAmiloride-sensitive epithelial sodium channelCell-free translation assaysShort NH2Transmembrane domainMembrane insertionHomologous subunitsXenopus laevis oocytesTranslation assaysSodium channelsGlycosylation sitesCOOH terminusCytoplasmic sideFunctional expressionTerminal endSubunitsHydrophilic NH2Laevis oocytesAlpha-rENaCEpithelial sodium channels
Rossier B, Canessa C, Schild L, Horisberger J. Epithelial sodium channels. Current Opinion In Nephrology & Hypertension 1994, 3: 487-496. PMID: 7804746, DOI: 10.1097/00041552-199409000-00003.Peer-Reviewed Original ResearchConceptsEpithelial sodium channelAmiloride-sensitive epithelial sodium channelSodium channelsNovel genesHeteromultimeric proteinsHomologous subunitsDistinct functionsRat epithelial sodium channelPrimary structureCation channelsBiophysical propertiesCritical roleTaste transductionTransductionGenesMechanotransductionSubunitsProteinCell distributionRegulation
1992
Primary sequence and functional expression of a novel ouabain-resistant Na,K-ATPase. The beta subunit modulates potassium activation of the Na,K-pump.
Jaisser F, Canessa C, Horisberger J, Rossier B. Primary sequence and functional expression of a novel ouabain-resistant Na,K-ATPase. The beta subunit modulates potassium activation of the Na,K-pump. Journal Of Biological Chemistry 1992, 267: 16895-16903. PMID: 1380956, DOI: 10.1016/s0021-9258(18)41869-8.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBase SequenceBlotting, NorthernBufo marinusCell LineCloning, MolecularFemaleGene LibraryHumansIsoenzymesMacromolecular SubstancesMolecular Sequence DataOligodeoxyribonucleotidesOligonucleotides, AntisenseOocytesOuabainPotassiumRecombinant ProteinsRNASequence Homology, Nucleic AcidSodium-Potassium-Exchanging ATPaseTranscription, GeneticUrinary BladderXenopus laevisConceptsOuabain-resistant phenotypeAlpha 1 isoformBeta subunitAmino acidsK-ATPase alphaBeta 1Alpha 1Alpha 1 beta 1Oocyte expression systemXenopus laevis oocyte expression systemSequence comparisonBladder cell linesK pumpTerminal borderC-terminusExtracellular potassium ionsPrimary sequenceExpression systemMolecular mechanismsOuabain resistanceBeta 3 isoformsOuabain-resistant NaExtracellular loopFunctional expressionSubunitsMutation of a cysteine in the first transmembrane segment of Na,K‐ATPase alpha subunit confers ouabain resistance.
Canessa C, Horisberger J, Louvard D, Rossier B. Mutation of a cysteine in the first transmembrane segment of Na,K‐ATPase alpha subunit confers ouabain resistance. The EMBO Journal 1992, 11: 1681-1687. PMID: 1316269, PMCID: PMC556624, DOI: 10.1002/j.1460-2075.1992.tb05218.x.Peer-Reviewed Original Research