2008
A proton‐independent function of ASIC in Ciona intestinalis
Coric T, Passamaneck Y, Zhang P, Di Gregorio A, Canessa C. A proton‐independent function of ASIC in Ciona intestinalis. The FASEB Journal 2008, 22: 945.4-945.4. DOI: 10.1096/fasebj.22.1_supplement.945.4.Peer-Reviewed Original ResearchCiona intestinalisAcid-sensitive ion channelsChordate nervous systemAscidian Ciona intestinalisLarval nervous systemPhysiological genomicsAdult nervous systemSequence similarityHigher vertebratesHeterologous systemsLarval neuronsSpliced formsASIC functionNervous systemLarval swimmingIon channelsASIC genesExtracellular protonsSodium channelsProton sensitivityIntestinalisMost neuronsSynaptic transmissionCionaVertebrates
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
2003
Distribution and regulation of expression of serum‐ and glucocorticoid‐induced kinase‐1 in the rat kidney
de la Rosa D, Coric T, Todorovic N, Shao D, Wang T, Canessa C. Distribution and regulation of expression of serum‐ and glucocorticoid‐induced kinase‐1 in the rat kidney. The Journal Of Physiology 2003, 551: 455-466. PMID: 12816971, PMCID: PMC2343216, DOI: 10.1113/jphysiol.2003.042903.Peer-Reviewed Original ResearchMeSH KeywordsAdrenalectomyAldosteroneAnimalsAntibodiesAntibody SpecificityBlotting, NorthernBlotting, WesternCells, CulturedDNA, ComplementaryElectrophoresis, Polyacrylamide GelEpithelial CellsGene Expression Regulation, EnzymologicGlucocorticoidsImmediate-Early ProteinsImmunoblottingIn Vitro TechniquesIsoenzymesKidneyKidney TubulesMicroscopy, FluorescenceNuclear ProteinsProtein Serine-Threonine KinasesRatsRats, Sprague-DawleyRNASubcellular FractionsTransfectionConceptsGlucocorticoid-induced kinase 1Kinase 1Ion channelsRegulation of expressionConstitutive high expressionBasolateral membraneRenal epithelial cellsSubcellular localizationLevel of expressionRegulation of levelsEpithelial ion channelsSGK1 proteinMammalian kidneyApical membraneDirect interactionSGK1Epithelial cellsWestern blottingHigh expressionExpressionExpression of SGK1ProteinRat kidneyTransportersPhysiological changes
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
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 ResearchConceptsSecond 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
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