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.
1994
An 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 mechanisms
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