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
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
The 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
Chapter 4 Structure–Function Relationship of Na,K-ATPase: The Digitalis Receptor
Canessa C, Jaisser F, Horisberger J, Rossier B. Chapter 4 Structure–Function Relationship of Na,K-ATPase: The Digitalis Receptor. Current Topics In Membranes 1994, 41: 71-85. DOI: 10.1016/s0070-2161(08)60454-2.Peer-Reviewed Original ResearchStructure-function relationshipsAmino acidsFirst transmembrane domainSite-directed mutagenesisK-ATPaseAmino acid residuesOuabain-sensitive cellsFunctional mutantsTransmembrane domainCellular processesDrug-binding sitesAromatic amino acidsDigitalis receptorWild typeContact sitesRandom mutationsOuabain resistanceΑ-subunitAcid residuesSite-specific ligandsFunctional assaysCardiac glycosidesCell linesOuabain analoguesK-ATPase activity
1992
Mutation 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