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
2005
SGK1 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
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 ResearchThe highly selective low-conductance epithelial Na channel of Xenopus laevis A6 kidney cells
Puoti A, May A, Canessa C, Horisberger J, Schild L, Rossier B. The highly selective low-conductance epithelial Na channel of Xenopus laevis A6 kidney cells. American Journal Of Physiology 1995, 269: c188-c197. PMID: 7631745, DOI: 10.1152/ajpcell.1995.269.1.c188.Peer-Reviewed Original Research
1994
Amiloride-sensitive epithelial Na+ channel is made of three homologous subunits
Canessa C, Schild L, Buell G, Thorens B, Gautschi I, Horisberger J, Rossier B. Amiloride-sensitive epithelial Na+ channel is made of three homologous subunits. Nature 1994, 367: 463-467. PMID: 8107805, DOI: 10.1038/367463a0.Peer-Reviewed Original ResearchConceptsEpithelial sodium channelRat epithelial sodium channelSodium channelsSodium reabsorptionSodium balanceDistal colonAmiloride-sensitive epithelial sodium channelPharmacological profileBlood volumeRenal tubulesRat epithelialExocrine glandsEpithelial cellsΑ-subunitDistal partNative channelsExpression cloningAldosteroneLungColon
1993
Mutation of a tyrosine in the H3-H4 ectodomain of Na,K-ATPase alpha subunit confers ouabain resistance.
Canessa C, Horisberger J, Rossier B. Mutation of a tyrosine in the H3-H4 ectodomain of Na,K-ATPase alpha subunit confers ouabain resistance. Journal Of Biological Chemistry 1993, 268: 17722-17726. PMID: 8394348, DOI: 10.1016/s0021-9258(17)46764-0.Peer-Reviewed Original ResearchAmino Acid SequenceAnimalsBase SequenceBinding SitesCell LineCloning, MolecularDogsFemaleKidneyKineticsMacromolecular SubstancesMolecular Sequence DataMutagenesis, Site-DirectedOligodeoxyribonucleotidesOocytesOuabainPeptide FragmentsPolymerase Chain ReactionProtein ConformationRecombinant ProteinsSequence Homology, Amino AcidSodium-Potassium-Exchanging ATPaseTime FactorsXenopus laevis
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