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 ResearchMeSH KeywordsAnimalsEpithelial CellsIon Channel GatingPatch-Clamp TechniquesRecombinant Fusion ProteinsSodium ChannelsXenopusConceptsSecond 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 affinity
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 regulationMutations
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: 4440-50. 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