2023
Phosphatases maintain low catalytic activity of SGK1: DNA damage resets the balance in favor of phosphorylation
Gu W, Zheng H, Canessa C. Phosphatases maintain low catalytic activity of SGK1: DNA damage resets the balance in favor of phosphorylation. Journal Of Biological Chemistry 2023, 299: 104941. PMID: 37343701, PMCID: PMC10372406, DOI: 10.1016/j.jbc.2023.104941.Peer-Reviewed Original ResearchMeSH KeywordsCell Line, TumorCell SurvivalDNA DamageEnzyme ActivationHumansPhosphoprotein PhosphatasesPhosphorylationProtein Serine-Threonine KinasesConceptsDNA-dependent protein kinaseCell survivalHsp90 chaperone complexDNA damage responseGlucocorticoid-induced kinase 1Inhibitor of phosphatasesChaperone complexGenotoxic stressDamage responseCatalytic subunitProtein kinaseNovel cancer therapiesKinase 1Stress conditionsDNA damageMolecular pathwaysSGK1 activityPP2ASGK1Cancer cellsDephosphorylationEndogenous inhibitorKinasePP5Phosphorylation
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 ResearchMeSH KeywordsAnimalsCell LineHumansImmediate-Early ProteinsIsoenzymesMiceMolecular WeightProtein BiosynthesisProtein Serine-Threonine KinasesRNA, MessengerSubstrate SpecificityTissue DistributionConceptsFunctional 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
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
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
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
1999
The Serum and Glucocorticoid Kinase sgk Increases the Abundance of Epithelial Sodium Channels in the Plasma Membrane of Xenopus Oocytes*
de la Rosa D, Zhang P, Náray-Fejes-Tóth A, Fejes-Tóth G, Canessa C. The Serum and Glucocorticoid Kinase sgk Increases the Abundance of Epithelial Sodium Channels in the Plasma Membrane of Xenopus Oocytes*. Journal Of Biological Chemistry 1999, 274: 37834-37839. PMID: 10608847, DOI: 10.1074/jbc.274.53.37834.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCell MembraneEpithelial Sodium ChannelsImmediate-Early ProteinsKineticsNuclear ProteinsOocytesProtein Serine-Threonine KinasesRatsRecombinant ProteinsSerineSodium ChannelsThreonineXenopus laevisConceptsCarboxyl terminusPlasma membraneEpithelial sodium channelSerine/threonineXenopus oocytesNumber of ENaCsGlucocorticoid-induced kinaseRenal epithelial cellsThreonine kinaseSodium channelsMembrane abundanceTyrosine residuesGamma subunitsSGKAbundance of ENaCCell surfacePhosphorylationTerminusAmiloride-sensitive sodium transportAbundanceSodium transportKinaseENaC.Epithelial cellsSubunitssgk Is an Aldosterone-induced Kinase in the Renal Collecting Duct EFFECTS ON EPITHELIAL Na+ CHANNELS*
Náray-Fejes-Tóth A, Canessa C, Cleaveland E, Aldrich G, Fejes-Tóth G. sgk Is an Aldosterone-induced Kinase in the Renal Collecting Duct EFFECTS ON EPITHELIAL Na+ CHANNELS*. Journal Of Biological Chemistry 1999, 274: 16973-16978. PMID: 10358046, DOI: 10.1074/jbc.274.24.16973.Peer-Reviewed Original ResearchMeSH KeywordsAldosteroneAmilorideAmino Acid SequenceAndrostanolsAnimalsElectric ConductivityEnzyme InductionImmediate-Early ProteinsKidney Tubules, CollectingMolecular Sequence DataNuclear ProteinsProtein Serine-Threonine KinasesRabbitsReceptors, MineralocorticoidRecombinant ProteinsRNA, MessengerSequence Homology, Amino AcidConceptsAddition of aldosteroneTarget cellsAldosterone-induced geneAldosterone-induced kinaseApical sodium channelsEarly phaseMineralocorticoid target cellsSodium reabsorptionMineralocorticoid receptorNative target cellsImmediate early genesAldosteroneStimulatory effectDuct cellsSodium channelsMRNA levelsDe novo protein synthesisRenal epitheliumPolymerase chain reaction-based subtractive hybridizationNovo protein synthesisEarly genesCellsDifferential display techniqueProtein synthesisKinase