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
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 degradationReticulumMotifPathwayUb
2000
Structure 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
Sodium 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. Histology And Histopathology 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
1998
Structure and function of the Mec-ENaC family of ion channels.
Fyfe G, Quinn A, Canessa C. Structure and function of the Mec-ENaC family of ion channels. Seminars In Nephrology 1998, 18: 138-51. PMID: 9541269.Peer-Reviewed Original ResearchConceptsIon channelsLittle amino acid identityCell type-dependent expressionAmino acid identityAcid identityDistinct tissuesEpithelial sodium channelFunction mutationsRecent discoveryProteinDifferential sensitivitySodium channelsSpecialized neuronsNew familyNociceptive painBlood pressureFamilyTissue injurySodium homeostasisSame common structureCommon ailmentsMechanical stimuliCloningTransductionDiuretic amiloride
1995
Hypertension 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 regulationMutationsCloning 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 oocytesSubunitsRelative expression of the human epithelial Na+ channel subunits in normal and cystic fibrosis airways
Burch L, Talbot C, Knowles M, Canessa C, Rossier B, Boucher R. Relative expression of the human epithelial Na+ channel subunits in normal and cystic fibrosis airways. American Journal Of Physiology 1995, 269: c511-c518. PMID: 7653534, DOI: 10.1152/ajpcell.1995.269.2.c511.Peer-Reviewed Original ResearchConceptsAirway epitheliumSuperficial epitheliumCF airwaysGamma-ENaC mRNACF airway diseaseENaC subunit mRNAsCystic fibrosis airway epitheliaCF airway epitheliaAirway diseaseSitu hybridization studiesDuctal epitheliumCF transmembrane conductance regulator (CFTR) proteinRibonuclease protection assaysAcinar epitheliumMolecular pathogenesisCystic fibrosisChannel mRNAInhibitory regulationSubunit mRNAsEpitheliumChannel subunitsRatio of alphaAirwayRelative expressionPathogenesisLiddle’s syndrome: Heritable human hypertension caused by mutations in the ß subnit of the epithelial sodium channel
Shimkets R, Warnock D, Bositis C, Nelson-Williams C, Hansson J, Schambelan M, Gill J, Ulick S, Milora R, Findling J, Canessa C, Rossier B, Lifton R, Corvol P. Liddle’s syndrome: Heritable human hypertension caused by mutations in the ß subnit of the epithelial sodium channel. Journal Of Endocrinological Investigation 1995, 18: 592-594. PMID: 9221280, DOI: 10.1007/bf03349775.Peer-Reviewed Original Research
1994
SCNN1, an Epithelial Cell Sodium Channel Gene in the Conserved Linkage Group on Mouse Chromosome 6 and Human Chromosome 12
Meisler M, Barrow L, Canessa C, Rossier B. SCNN1, an Epithelial Cell Sodium Channel Gene in the Conserved Linkage Group on Mouse Chromosome 6 and Human Chromosome 12. Genomics 1994, 24: 185-186. PMID: 7896277, DOI: 10.1006/geno.1994.1599.Peer-Reviewed Original ResearchAn SH3 binding region in the epithelial Na+ channel (alpha rENaC) mediates its localization at the apical membrane.
Rotin D, Bar‐Sagi D, O'Brodovich H, Merilainen J, Lehto V, Canessa C, Rossier B, Downey G. An SH3 binding region in the epithelial Na+ channel (alpha rENaC) mediates its localization at the apical membrane. The EMBO Journal 1994, 13: 4440-4450. PMID: 7925286, PMCID: PMC395375, DOI: 10.1002/j.1460-2075.1994.tb06766.x.Peer-Reviewed Original ResearchConceptsC-terminal regionAlpha-spectrinSH3 domainCytoskeletal interactionsFusion proteinTerminal proline-rich regionAlpha-rENaCApical membranePolarized epithelial cellsProline-rich sequenceN-terminal proteinProline-rich regionEpithelial cellsApical membrane localizationCytoskeletal protein ankyrinProper channel functionPrimary rat alveolar epithelial cellsEpithelial cell lysatesMembrane localizationRat alveolar epithelial cellsProtein ankyrinApical localizationPlasma membraneRecombinant fusion proteinMolecular mechanismsEpithelial 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 expressionSubunits