2014
Recurrent activating mutation in PRKACA in cortisol-producing adrenal tumors
Goh G, Scholl UI, Healy JM, Choi M, Prasad ML, Nelson-Williams C, Kunstman JW, Korah R, Suttorp AC, Dietrich D, Haase M, Willenberg HS, Stålberg P, Hellman P, Åkerström G, Björklund P, Carling T, Lifton RP. Recurrent activating mutation in PRKACA in cortisol-producing adrenal tumors. Nature Genetics 2014, 46: 613-617. PMID: 24747643, PMCID: PMC4074779, DOI: 10.1038/ng.2956.Peer-Reviewed Original ResearchAdolescentAdrenal Gland NeoplasmsAdultAgedAmino Acid SequenceBase SequenceCdc42 GTP-Binding ProteinCell ProliferationCyclic AMP-Dependent Protein Kinase Catalytic SubunitsCyclin-Dependent Kinase Inhibitor p16DNA Copy Number VariationsExomeFemaleGene DeletionGene DosageHEK293 CellsHumansHydrocortisoneMaleMiddle AgedMolecular Sequence DataMutationPhosphorylationSequence Analysis, DNASequence Homology, Amino Acid
2013
Mineralocorticoid Receptor Phosphorylation Regulates Ligand Binding and Renal Response to Volume Depletion and Hyperkalemia
Shibata S, Rinehart J, Zhang J, Moeckel G, Castañeda-Bueno M, Stiegler AL, Boggon TJ, Gamba G, Lifton RP. Mineralocorticoid Receptor Phosphorylation Regulates Ligand Binding and Renal Response to Volume Depletion and Hyperkalemia. Cell Metabolism 2013, 18: 660-671. PMID: 24206662, PMCID: PMC3909709, DOI: 10.1016/j.cmet.2013.10.005.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAngiotensin IIAnimalsChlorocebus aethiopsCOS CellsCytoplasmElectrolytesHumansHyperkalemiaKidneyLigandsMiceMolecular Sequence DataPhosphoprotein PhosphatasesPhosphorylationPhosphoserinePotassium, DietaryProtein Serine-Threonine KinasesProtein TransportRatsReceptors, MineralocorticoidSignal TransductionTranscriptional ActivationConceptsVolume depletionMineralocorticoid receptorAldosterone-dependent increaseHormone receptor activityNuclear hormone receptor activityMR activationRenal responseDistinct adaptive responsesAngiotensin IIDistal nephronCl reabsorptionHyperkalemiaMR ligand-binding domainReceptor activityApical proton pumpPlasma volumeReceptor bindingHomeostatic responseNuclear receptorsReceptor phosphorylation
2012
Mutations in kelch-like 3 and cullin 3 cause hypertension and electrolyte abnormalities
Boyden LM, Choi M, Choate KA, Nelson-Williams CJ, Farhi A, Toka HR, Tikhonova IR, Bjornson R, Mane SM, Colussi G, Lebel M, Gordon RD, Semmekrot BA, Poujol A, Välimäki MJ, De Ferrari ME, Sanjad SA, Gutkin M, Karet FE, Tucci JR, Stockigt JR, Keppler-Noreuil KM, Porter CC, Anand SK, Whiteford ML, Davis ID, Dewar SB, Bettinelli A, Fadrowski JJ, Belsha CW, Hunley TE, Nelson RD, Trachtman H, Cole TR, Pinsk M, Bockenhauer D, Shenoy M, Vaidyanathan P, Foreman JW, Rasoulpour M, Thameem F, Al-Shahrouri HZ, Radhakrishnan J, Gharavi AG, Goilav B, Lifton RP. Mutations in kelch-like 3 and cullin 3 cause hypertension and electrolyte abnormalities. Nature 2012, 482: 98-102. PMID: 22266938, PMCID: PMC3278668, DOI: 10.1038/nature10814.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingAmino Acid SequenceAnimalsBase SequenceBlood PressureCarrier ProteinsCohort StudiesCullin ProteinsElectrolytesExonsFemaleGene Expression ProfilingGenes, DominantGenes, RecessiveGenotypeHomeostasisHumansHydrogen-Ion ConcentrationHypertensionMaleMiceMicrofilament ProteinsModels, MolecularMolecular Sequence DataMutationPhenotypePotassiumPseudohypoaldosteronismSodium ChlorideWater-Electrolyte Imbalance
2010
Mitotic Recombination in Patients with Ichthyosis Causes Reversion of Dominant Mutations in KRT10
Choate KA, Lu Y, Zhou J, Choi M, Elias PM, Farhi A, Nelson-Williams C, Crumrine D, Williams ML, Nopper AJ, Bree A, Milstone LM, Lifton RP. Mitotic Recombination in Patients with Ichthyosis Causes Reversion of Dominant Mutations in KRT10. Science 2010, 330: 94-97. PMID: 20798280, PMCID: PMC3085938, DOI: 10.1126/science.1192280.Peer-Reviewed Original ResearchAmino Acid SequenceCell NucleolusChromosome MappingChromosomes, Human, Pair 17FemaleFrameshift MutationHumansIchthyosiform Erythroderma, CongenitalIntermediate FilamentsKeratin-10KeratinsLoss of HeterozygosityMaleMitosisMolecular Sequence DataMosaicismMutant ProteinsRecombination, GeneticSelection, GeneticSkin
2009
Sites of Regulated Phosphorylation that Control K-Cl Cotransporter Activity
Rinehart J, Maksimova YD, Tanis JE, Stone KL, Hodson CA, Zhang J, Risinger M, Pan W, Wu D, Colangelo CM, Forbush B, Joiner CH, Gulcicek EE, Gallagher PG, Lifton RP. Sites of Regulated Phosphorylation that Control K-Cl Cotransporter Activity. Cell 2009, 138: 525-536. PMID: 19665974, PMCID: PMC2811214, DOI: 10.1016/j.cell.2009.05.031.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAmino Acid SubstitutionAnimalsHumansMiceMolecular Sequence DataPhosphorylationSequence AlignmentSymportersConceptsIntrinsic transport activityK-Cl cotransporterTransport activityCell volume regulationRegulated phosphorylationRNA interferenceAlanine substitutionsCultured cellsHomologous sitesKCC activityCl exitWNK1 expressionNeonatal mouse brainVolume regulationNeuronal functionHypotonic conditionsActive cotransportPhosphorylationIntracellular chloride concentrationCotransporter activityKCC3Human red blood cellsKCC2 activationFundamental roleMouse brain