2007
Multiple Translational Isoforms Give Functional Specificity to Serum- and Glucocorticoid-induced Kinase 1
Arteaga MF, de la Rosa D, Alvarez JA, Canessa CM. Multiple Translational Isoforms Give Functional Specificity to Serum- and Glucocorticoid-induced Kinase 1. Molecular Biology Of The Cell 2007, 18: 2072-2080. PMID: 17377066, PMCID: PMC1877090, DOI: 10.1091/mbc.e06-10-0968.Peer-Reviewed Original ResearchConceptsFunctional specificityKinase 1Core kinase domainGlycogen synthase kinase-3betaAlternative translation initiationDifferent cellular compartmentsSynthase kinase-3betaGlucocorticoid-induced kinase 1Different N-terminiActivation of SGK1ER membraneTranslation initiationCellular compartmentsKinase domainKinase-3betaUbiquitous kinaseTranscriptional factorsN-terminusDiverse processesEpithelial sodium channelLong isoformShort isoformER stressCell survivalTranslational isoforms
2006
An amphipathic helix targets serum and glucocorticoid-induced kinase 1 to the endoplasmic reticulum-associated ubiquitin-conjugation machinery
Arteaga MF, Wang L, Ravid T, Hochstrasser M, Canessa CM. An amphipathic helix targets serum and glucocorticoid-induced kinase 1 to the endoplasmic reticulum-associated ubiquitin-conjugation machinery. Proceedings Of The National Academy Of Sciences Of The United States Of America 2006, 103: 11178-11183. PMID: 16847254, PMCID: PMC1544061, DOI: 10.1073/pnas.0604816103.Peer-Reviewed Original ResearchConceptsGlucocorticoid-induced kinase 1Kinase 1Endoplasmic reticulumRapid protein turnoverUbiquitin conjugation machineryHydrophobic motifER localizationMammalian cellsSubcellular localizationCytosolic substratesGene transcriptionProtein turnoverDegradation systemCell survivalStress conditionsReduction of hydrophobicityIon channelsSGK1HRD1Epithelial cellsRapid degradationReticulumMotifPathwayUbGating of Acid-sensitive Ion Channel-1: Release of Ca2+ Block vs. Allosteric Mechanism
Zhang P, Sigworth FJ, Canessa CM. Gating of Acid-sensitive Ion Channel-1: Release of Ca2+ Block vs. Allosteric Mechanism. The Journal Of General Physiology 2006, 127: 109-117. PMID: 16418400, PMCID: PMC2151491, DOI: 10.1085/jgp.200509396.Peer-Reviewed Original ResearchAcid Sensing Ion ChannelsAllosteric RegulationAnimalsBatrachoidiformesBinding SitesCalciumElectric ConductivityFemaleGene ExpressionIon Channel GatingMembrane ProteinsModels, BiologicalNerve Tissue ProteinsOocytesPatch-Clamp TechniquesProtein ConformationProtonsSodium ChannelsTime FactorsXenopus laevis
2005
Proton sensitivity of ASIC1 appeared with the rise of fishes by changes of residues in the region that follows TM1 in the ectodomain of the channel
Coric T, Zheng D, Gerstein M, Canessa CM. Proton sensitivity of ASIC1 appeared with the rise of fishes by changes of residues in the region that follows TM1 in the ectodomain of the channel. The Journal Of Physiology 2005, 568: 725-735. PMID: 16002453, PMCID: PMC1464184, DOI: 10.1113/jphysiol.2005.087734.Peer-Reviewed Original ResearchMeSH KeywordsAcid Sensing Ion ChannelsAmino Acid SequenceAmino AcidsAnimalsEvolution, MolecularFishesHydrogen-Ion ConcentrationIon Channel GatingMembrane ProteinsMolecular Sequence DataNerve Tissue ProteinsProtein Structure, TertiaryProtonsSequence Homology, Amino AcidSodium ChannelsSpecies SpecificityStructure-Activity RelationshipConceptsAmino acid conservationChanges of residuesProton sensitivityMammalian nervous systemChordate lineageEarly vertebratesFunctional chimerasMammalian counterpartsLower vertebratesAllosteric changesProtein sequencesExtracellular domainSequence analysisDifferent speciesRat sequenceRat channelKinetics of activationStructural determinantsDistinct kineticsVertebratesASIC1 channelsMembrane potentialChimerasSharksEctodomainSGK1 activates Na+-K+-ATPase in amphibian renal epithelial cells
de la Rosa D, Gimenez I, Forbush B, Canessa CM. SGK1 activates Na+-K+-ATPase in amphibian renal epithelial cells. American Journal Of Physiology - Cell Physiology 2005, 290: c492-c498. PMID: 16192298, DOI: 10.1152/ajpcell.00556.2004.Peer-Reviewed Original ResearchConceptsRenal epithelial cellsEpithelial cellsEffects of aldosteroneCell linesActivation of ENaCGlucocorticoid-induced kinase 1Epithelial cell lineRenal epithelial cell lineAldosteroneSGK1 expressionSame cell lineSubunit abundanceSGK1Channel activityTotal proteinImportant regulatorKinase 1Tetracycline-inducible promoterActivationCellsApical membraneATPase activityPrevious studiesATPase functionChronic
2003
Distribution and regulation of expression of serum‐ and glucocorticoid‐induced kinase‐1 in the rat kidney
de la Rosa D, Coric T, Todorovic N, Shao D, Wang T, Canessa C. Distribution and regulation of expression of serum‐ and glucocorticoid‐induced kinase‐1 in the rat kidney. The Journal Of Physiology 2003, 551: 455-466. PMID: 12816971, PMCID: PMC2343216, DOI: 10.1113/jphysiol.2003.042903.Peer-Reviewed Original ResearchMeSH KeywordsAdrenalectomyAldosteroneAnimalsAntibodiesAntibody SpecificityBlotting, NorthernBlotting, WesternCells, CulturedDNA, ComplementaryElectrophoresis, Polyacrylamide GelEpithelial CellsGene Expression Regulation, EnzymologicGlucocorticoidsImmediate-Early ProteinsImmunoblottingIn Vitro TechniquesIsoenzymesKidneyKidney TubulesMicroscopy, FluorescenceNuclear ProteinsProtein Serine-Threonine KinasesRatsRats, Sprague-DawleyRNASubcellular FractionsTransfectionConceptsGlucocorticoid-induced kinase 1Kinase 1Ion channelsRegulation of expressionConstitutive high expressionBasolateral membraneRenal epithelial cellsSubcellular localizationLevel of expressionRegulation of levelsEpithelial ion channelsSGK1 proteinMammalian kidneyApical membraneDirect interactionSGK1Epithelial cellsWestern blottingHigh expressionExpressionExpression of SGK1ProteinRat kidneyTransportersPhysiological changes
2001
Single-Channel Properties of Recombinant Acid-Sensitive Ion Channels Formed by the Subunits Asic2 and Asic3 from Dorsal Root Ganglion Neurons Expressed in Xenopus Oocytes
Zhang P, Canessa C. Single-Channel Properties of Recombinant Acid-Sensitive Ion Channels Formed by the Subunits Asic2 and Asic3 from Dorsal Root Ganglion Neurons Expressed in Xenopus Oocytes. The Journal Of General Physiology 2001, 117: 563-572. PMID: 11382806, PMCID: PMC2232399, DOI: 10.1085/jgp.117.6.563.Peer-Reviewed Original Research
2000
Heterologous expression of a mammalian epithelial sodium channel in yeast
Gupta S, Canessa C. Heterologous expression of a mammalian epithelial sodium channel in yeast. FEBS Letters 2000, 481: 77-80. PMID: 10984619, DOI: 10.1016/s0014-5793(00)01977-3.Peer-Reviewed Original ResearchMeSH KeywordsAmilorideAnimalsBlotting, WesternCarrier ProteinsCell DivisionCell MembraneCytoplasmic GranulesEpithelial Sodium ChannelsGene Expression Regulation, FungalHot TemperatureMembrane ProteinsMicrobial Sensitivity TestsMutationOsmolar ConcentrationRatsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSodium Channel BlockersSodium ChannelsSodium ChlorideVesicular Transport ProteinsConceptsEpithelial sodium channelYeast SaccharomycesHeterologous expressionSecretory pathwayBeta-ENaCPlasma membraneSodium channelsRat epithelial sodium channelBeta subunitSecretory systemYeast strainYeastParent strainWestern blotting techniquesENaCBlotting techniquesSalt sensitivityMutantsSaccharomycesStructure and Regulation of Amiloride-Sensitive Sodium Channels
de la Rosa D, Canessa C, Fyfe G, Zhang P. Structure and Regulation of Amiloride-Sensitive Sodium Channels. Annual Review Of Physiology 2000, 62: 573-594. PMID: 10845103, DOI: 10.1146/annurev.physiol.62.1.573.Peer-Reviewed Original Research
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 cellsSubunitssgk Is an Aldosterone-induced Kinase in the Renal Collecting Duct EFFECTS ON EPITHELIAL Na+ CHANNELS*
Náray-Fejes-Tóth A, Canessa C, Cleaveland E, Aldrich G, Fejes-Tóth G. sgk Is an Aldosterone-induced Kinase in the Renal Collecting Duct EFFECTS ON EPITHELIAL Na+ CHANNELS*. Journal Of Biological Chemistry 1999, 274: 16973-16978. PMID: 10358046, DOI: 10.1074/jbc.274.24.16973.Peer-Reviewed Original ResearchMeSH KeywordsAldosteroneAmilorideAmino Acid SequenceAndrostanolsAnimalsElectric ConductivityEnzyme InductionImmediate-Early ProteinsKidney Tubules, CollectingMolecular Sequence DataNuclear ProteinsProtein Serine-Threonine KinasesRabbitsReceptors, MineralocorticoidRecombinant ProteinsRNA, MessengerSequence Homology, Amino AcidConceptsAddition of aldosteroneTarget cellsAldosterone-induced geneAldosterone-induced kinaseApical sodium channelsEarly phaseMineralocorticoid target cellsSodium reabsorptionMineralocorticoid receptorNative target cellsImmediate early genesAldosteroneStimulatory effectDuct cellsSodium channelsMRNA levelsDe novo protein synthesisRenal epitheliumPolymerase chain reaction-based subtractive hybridizationNovo protein synthesisEarly genesCellsDifferential display techniqueProtein synthesisKinase
1998
Subunit Composition Determines the Single Channel Kinetics of the Epithelial Sodium Channel
Fyfe G, Canessa C. Subunit Composition Determines the Single Channel Kinetics of the Epithelial Sodium Channel. The Journal Of General Physiology 1998, 112: 423-432. PMID: 9758861, PMCID: PMC2229421, DOI: 10.1085/jgp.112.4.423.Peer-Reviewed Original ResearchIn 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.
1997
The Activity of the Epithelial Sodium Channel Is Regulated by Clathrin-mediated Endocytosis*
Shimkets R, Lifton R, Canessa C. The Activity of the Epithelial Sodium Channel Is Regulated by Clathrin-mediated Endocytosis*. Journal Of Biological Chemistry 1997, 272: 25537-25541. PMID: 9325269, DOI: 10.1074/jbc.272.41.25537.Peer-Reviewed Original ResearchConceptsWild-type channelsDynamin mutantPlasma membraneEpithelial sodium channelClathrin-coated pit-mediated endocytosisLiddle mutationClathrin-coated pit pathwayDominant-negative dynamin mutantPit-mediated endocytosisChannel activityLoss of endocytosisActivity of channelsLiddle's syndromePy domainsCarboxyl terminusSodium channelsWild-type ENaCBrefeldin APit pathwayEndocytosisCell surfaceSpecific inhibitorXenopus oocytesNormal turnoverMutationsDiversity of Channels Generated by Different Combinations of Epithelial Sodium Channel Subunits
McNicholas C, Canessa C. Diversity of Channels Generated by Different Combinations of Epithelial Sodium Channel Subunits. The Journal Of General Physiology 1997, 109: 681-692. PMID: 9222895, PMCID: PMC2217047, DOI: 10.1085/jgp.109.6.681.Peer-Reviewed Original ResearchNoncoordinated expression of alpha-, beta-, and gamma-subunit mRNAs of epithelial Na+ channel along rat respiratory tract
Farman N, Talbot C, Boucher R, Fay M, Canessa C, Rossier B, Bonvalet J. Noncoordinated expression of alpha-, beta-, and gamma-subunit mRNAs of epithelial Na+ channel along rat respiratory tract. American Journal Of Physiology 1997, 272: c131-c141. PMID: 9038819, DOI: 10.1152/ajpcell.1997.272.1.c131.Peer-Reviewed Original ResearchConceptsRespiratory tractRat respiratory tractEpithelial cellsUpper airway epithelial cellsAirway epithelial cellsRespiratory epithelial cellsGamma-subunit mRNAType II pneumocytesRenal collecting tubulesBronchiolar epitheliumDistal colonCollecting tubuleRat lungSubunit expressionAlveolar cellsLarge prevalenceTracheal epitheliumGland ductsCellular expressionEpithelial surfaceMRNA levelsRespiratory physiologyGland aciniTractLuminal surface
1995
Amiloride-sensitive sodium channels in confluent M-1 mouse cortical collecting duct cells
Letz B, Ackermann A, Canessa C, Rossier B, Korbmacher C. Amiloride-sensitive sodium channels in confluent M-1 mouse cortical collecting duct cells. The Journal Of Membrane Biology 1995, 148: 127-141. PMID: 8606362, DOI: 10.1007/bf00207269.Peer-Reviewed Original ResearchExpression cloning of the epithelial sodium channel
Canessa C, Horisberger J, Schild L, Rossier B. Expression cloning of the epithelial sodium channel. Kidney International 1995, 48: 950-955. PMID: 8569104, DOI: 10.1038/ki.1995.376.Peer-Reviewed Original ResearchHypertension caused by a truncated epithelial sodium channel γ subunit: genetic heterogeneity of Liddle syndrome
Hansson J, Nelson-Williams C, Suzuki H, Schild L, Shimkets R, Lu Y, Canessa C, Iwasaki T, Rossier B, Lifton R. Hypertension caused by a truncated epithelial sodium channel γ subunit: genetic heterogeneity of Liddle syndrome. Nature Genetics 1995, 11: 76-82. PMID: 7550319, DOI: 10.1038/ng0995-76.Peer-Reviewed Original ResearchMeSH KeywordsAdolescentAdultAldosteroneAllelesAmino Acid SequenceAnimalsBase SequenceCodonEpithelial Sodium ChannelsGene Expression RegulationGenesGenes, DominantHumansHypertensionHypokalemiaIon Channel GatingKidney Tubules, ProximalMiddle AgedMolecular Sequence DataMutagenesis, Site-DirectedMutationOocytesPedigreeRatsRecombinant Fusion ProteinsReninSequence AlignmentSequence Homology, Amino AcidSodium ChannelsSodium, DietarySyndromeTerminator Regions, GeneticXenopus laevisConceptsLiddle's syndromeRenal epithelial sodium channelEpithelial Sodium Channel γ-SubunitSalt-sensitive formsChannel activityChannel γ subunitBlood pressureDietary saltEpithelial sodium channelHuman hypertensionSyndromeGenetic heterogeneityHypertensionSodium channelsIndependent roleConstitutive activationΓ subunitMendelian disordersNegative regulationMutations