2023
Phosphatases maintain low catalytic activity of SGK1: DNA damage resets the balance in favor of phosphorylation
Gu W, Zheng H, Canessa C. Phosphatases maintain low catalytic activity of SGK1: DNA damage resets the balance in favor of phosphorylation. Journal Of Biological Chemistry 2023, 299: 104941. PMID: 37343701, PMCID: PMC10372406, DOI: 10.1016/j.jbc.2023.104941.Peer-Reviewed Original ResearchConceptsDNA-dependent protein kinaseCell survivalHsp90 chaperone complexDNA damage responseGlucocorticoid-induced kinase 1Inhibitor of phosphatasesChaperone complexGenotoxic stressDamage responseCatalytic subunitProtein kinaseNovel cancer therapiesKinase 1Stress conditionsDNA damageMolecular pathwaysSGK1 activityPP2ASGK1Cancer cellsDephosphorylationEndogenous inhibitorKinasePP5Phosphorylation
2019
A Mechanism for Desensitization of all Three Functional Mammalian Acid Sensing Ion Channels
Wu Y, Chen Z, Canessa C. A Mechanism for Desensitization of all Three Functional Mammalian Acid Sensing Ion Channels. Biophysical Journal 2019, 116: 36a. DOI: 10.1016/j.bpj.2018.11.237.Peer-Reviewed Original Research
2013
Heterogeneous nuclear ribonucleoprotein A2/B1 is a novel aldosterone target gene in the rat distal colon epithelium
de la Rosa D, Hernandez‐Diaz I, Morales S, Hernandez G, Salido E, Canessa C, Giraldez T. Heterogeneous nuclear ribonucleoprotein A2/B1 is a novel aldosterone target gene in the rat distal colon epithelium. The FASEB Journal 2013, 27: 1148.8-1148.8. DOI: 10.1096/fasebj.27.1_supplement.1148.8.Peer-Reviewed Original ResearchHnRNP A2/B1A2/B1Distal colonTarget tissuesAldosterone target tissuesHnRNP A2/B1 expressionRat distal colonRenal distal tubulesAldosterone target geneExtracellular volume homeostasisHeterogeneous nuclear ribonucleoprotein A2/B1Aldosterone levelsAcute increaseDistal colon epitheliumMineralocorticoid receptorDistal tubulesRat distal colon epitheliumHnRNP A2/B1 mRNAEpithelial targetsVolume homeostasisColon epitheliumB1 expressionEpithelial NaProtein expressionCell proliferation
2011
D433 Does Not Determine Ion Selectivity in ASIC1
Li T, Yang Y, Canessa C. D433 Does Not Determine Ion Selectivity in ASIC1. Biophysical Journal 2011, 100: 25a. DOI: 10.1016/j.bpj.2010.12.343.Peer-Reviewed Original Research
2010
The β1-β2 Linker in the Extracellular Domain of ASIC1 Determines Desensitization of ASIC1
Li T, Canessa C. The β1-β2 Linker in the Extracellular Domain of ASIC1 Determines Desensitization of ASIC1. Biophysical Journal 2010, 98: 702a. DOI: 10.1016/j.bpj.2009.12.3854.Peer-Reviewed Original Research
2009
Applications of Tissue Microarrays in Renal Physiology and Pathology
Mobasheri A, Cathro H, German A, Marples D, Martín‐vasallo P, Canessa C. Applications of Tissue Microarrays in Renal Physiology and Pathology. 2009, 97-118. DOI: 10.1002/9783527628612.ch8.Peer-Reviewed Original Research
2008
A proton‐independent function of ASIC in Ciona intestinalis
Coric T, Passamaneck Y, Zhang P, Di Gregorio A, Canessa C. A proton‐independent function of ASIC in Ciona intestinalis. The FASEB Journal 2008, 22: 945.4-945.4. DOI: 10.1096/fasebj.22.1_supplement.945.4.Peer-Reviewed Original ResearchCiona intestinalisAcid-sensitive ion channelsChordate nervous systemAscidian Ciona intestinalisLarval nervous systemPhysiological genomicsAdult nervous systemSequence similarityHigher vertebratesHeterologous systemsLarval neuronsSpliced formsASIC functionNervous systemLarval swimmingIon channelsASIC genesExtracellular protonsSodium channelsProton sensitivityIntestinalisMost neuronsSynaptic transmissionCionaVertebrates
2007
Multiple translational isoforms give functional specificity to serum‐ and glucocorticoid‐induced kinase 1 (Sgk1)
Arteaga M, Canessa C. Multiple translational isoforms give functional specificity to serum‐ and glucocorticoid‐induced kinase 1 (Sgk1). The FASEB Journal 2007, 21: a547-a548. DOI: 10.1096/fasebj.21.5.a547-d.Peer-Reviewed Original ResearchN-terminusFunctional specificityEvolutionary distant speciesCore kinase domainFOXO transcriptional factorAlternative translation initiationNumerous cellular processesDifferent cellular compartmentsGlucocorticoid-induced kinase 1Glycogen synthase kinase 3bDiversity of functionsDifferent N-terminiDistant speciesER membraneCellular processesTranslation initiationSingle kinaseCellular compartmentsKinase domainT kinaseTranscriptional factorsDistinct substratesKinase 1ER stressCell survivalMultiple 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 cellsSubunitsSodium transport systems in human chondrocytes. II. Expression of ENaC, Na+/K+/2Cl- cotransporter and Na+/H+ exchangers in healthy and arthritic chondrocytes.
Trujillo E, Alvarez de la Rosa D, Mobasheri A, González T, Canessa C, Martín-Vasallo P. Sodium transport systems in human chondrocytes. II. Expression of ENaC, Na+/K+/2Cl- cotransporter and Na+/H+ exchangers in healthy and arthritic chondrocytes. Cellular And Molecular Biology 1999, 14: 1023-31. PMID: 10506918, DOI: 10.14670/hh-14.1023.Peer-Reviewed Original ResearchConceptsRheumatoid arthritisHuman chondrocytesArthritic chondrocytesArthritic cartilageENaC protein levelsSodium-dependent transport systemExpression of ENaCSodium transport systemsEpithelial sodium channelHealthy individualsIntracellular pH regulationOA cartilageQuantities of alphaSodium channelsProtein levelsNHE isoformsBeta subunitSodium concentrationOsteoarthritisRelative expressionHuman cartilageAlphaCartilageEntry mechanismChondrocytes