2014
Rare Human Nicotinic Acetylcholine Receptor α4 Subunit (CHRNA4) Variants Affect Expression and Function of High-Affinity Nicotinic Acetylcholine Receptors
McClure-Begley TD, Papke RL, Stone KL, Stokes C, Levy AD, Gelernter J, Xie P, Lindstrom J, Picciotto MR. Rare Human Nicotinic Acetylcholine Receptor α4 Subunit (CHRNA4) Variants Affect Expression and Function of High-Affinity Nicotinic Acetylcholine Receptors. Journal Of Pharmacology And Experimental Therapeutics 2014, 348: 410-420. PMID: 24385388, PMCID: PMC3935145, DOI: 10.1124/jpet.113.209767.Peer-Reviewed Original ResearchConceptsNicotinic acetylcholine receptorsRare variantsSingle amino acid substitutionLaevis oocytesAmino acid substitutionsΑ4β2 nAChRsAcetylcholine receptorsIntracellular interactomesHEK-293 cellsX. laevis oocytesProteomic analysisGenetic variationHuman α4β2 nAChRsXenopus laevis oocytesVoltage-clamp electrophysiologyNeuronal nicotinic acetylcholine receptorsHigh-affinity nicotinic acetylcholine receptorsSubcellular distributionAcid substitutionsΑ4 nAChR subunitCohort of smokersEffects of nicotineNAChR subunitsCommon variantsΑ4 nAChR
2012
Embryonic poly(A)-binding protein (ePAB) phosphorylation is required for Xenopus oocyte maturation
Friend K, Brook M, Bezirci FB, Sheets MD, Gray NK, Seli E. Embryonic poly(A)-binding protein (ePAB) phosphorylation is required for Xenopus oocyte maturation. Biochemical Journal 2012, 445: 93-100. PMID: 22497250, PMCID: PMC3955212, DOI: 10.1042/bj20120304.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBlotting, WesternCytoplasmFemaleFluorescent Antibody TechniqueGene Expression Regulation, DevelopmentalImmunoprecipitationMutationOocytesOogenesisPhosphorylationPoly APoly(A)-Binding ProteinsPolyadenylationProtein BiosynthesisProtein Processing, Post-TranslationalRNA, MessengerXenopus laevisXenopus ProteinsConceptsCytoplasmic polyadenylationOocyte maturationPost-transcriptional regulatorsEarly embryonic developmentPost-translational modificationsXenopus oocyte maturationMaternal mRNAsProtein phosphorylationResidue clustersTranslational activationEmbryonic developmentXenopus laevis oocytesProtein activityPhosphorylationFirst insightLaevis oocytesPolyadenylationInherent abilityEPABMaturationPhosphoproteinRegulatorMutationsMRNAOocytes
2011
Divergent CFTR orthologs respond differently to the channel inhibitors CFTRinh-172, glibenclamide, and GlyH-101
Stahl M, Stahl K, Brubacher MB, Forrest JN. Divergent CFTR orthologs respond differently to the channel inhibitors CFTRinh-172, glibenclamide, and GlyH-101. American Journal Of Physiology - Cell Physiology 2011, 302: c67-c76. PMID: 21940661, PMCID: PMC3328903, DOI: 10.1152/ajpcell.00225.2011.Peer-Reviewed Original ResearchConceptsCystic fibrosis transmembrane conductance regulatorGlyH-101Expression studiesChannel proteinsCFTR chloride channel proteinFibrosis transmembrane conductance regulatorChloride channel proteinSite-directed mutagenesisShark rectal glandAmino acid residuesTransmembrane conductance regulatorDifferent orthologsSingle amino acidPrevious site-directed mutagenesisOocyte expression studiesThree-dimensional structureRegulatory regionsXenopus laevis oocytesCFTR proteinAdditional residuesConductance regulatorOrthologsAcid residuesRectal glandSpecific inhibitorWNK2 Kinase Is a Novel Regulator of Essential Neuronal Cation-Chloride Cotransporters*
Rinehart J, Vázquez N, Kahle KT, Hodson CA, Ring AM, Gulcicek EE, Louvi A, Bobadilla NA, Gamba G, Lifton RP. WNK2 Kinase Is a Novel Regulator of Essential Neuronal Cation-Chloride Cotransporters*. Journal Of Biological Chemistry 2011, 286: 30171-30180. PMID: 21733846, PMCID: PMC3191056, DOI: 10.1074/jbc.m111.222893.Peer-Reviewed Original ResearchConceptsCation-chloride cotransportersSerine-threonine phosphorylationKinase-dependent mannerMammalian brainCell volume regulationSer-383Protein complexesRegulatory cascadeCotransporter regulationXenopus laevis oocytesNovel regulatorWNK2KinaseLaevis oocytesVolume regulationCl accumulationRecognition sitesWNKIntracellular concentrationRegulationSPAKAdult brainThalamic relay cellsThiazide-sensitive NCCMass spectrometry studiesPosttranscriptional activation of gene expression in Xenopus laevis oocytes by microRNA–protein complexes (microRNPs)
Mortensen RD, Serra M, Steitz JA, Vasudevan S. Posttranscriptional activation of gene expression in Xenopus laevis oocytes by microRNA–protein complexes (microRNPs). Proceedings Of The National Academy Of Sciences Of The United States Of America 2011, 108: 8281-8286. PMID: 21536868, PMCID: PMC3100953, DOI: 10.1073/pnas.1105401108.Peer-Reviewed Original ResearchConceptsMicroRNA–protein complexesProtein kinase AIIXenopus laevis oocytesImmature Xenopus laevis oocytesGene expression activationMammalian cell linesLaevis oocytesHuman Ago2Target reporterMammalian cellsExpression activationMyt1 kinaseGene expressionPosttranscriptional activationRegulated expressionSpecific mRNAsPhysiological relevanceQuiescent cellsMicroRNAsOocyte stateCell linesOocytesReporterCAMP levelsExpressionRare mutations in the human Na-K-Cl cotransporter (NKCC2) associated with lower blood pressure exhibit impaired processing and transport function
Monette MY, Rinehart J, Lifton RP, Forbush B. Rare mutations in the human Na-K-Cl cotransporter (NKCC2) associated with lower blood pressure exhibit impaired processing and transport function. American Journal Of Physiology. Renal Physiology 2011, 300: f840-f847. PMID: 21209010, PMCID: PMC3074999, DOI: 10.1152/ajprenal.00552.2010.Peer-Reviewed Original ResearchConceptsHEK-293 cellsNa-K-Cl cotransporterTransport functionMajor salt transport pathwayPlasma membrane localizationHEK cellsLow transport activitySequence conservationMembrane localizationProtein functionHeterologous expressionXenopus laevis oocytesImportant residuesMutantsRenal salt reabsorptionMolecular mechanismsIndependent mutationsConstitutive activityTransport activityBlood pressureFunctional consequencesImpaired transport functionSuch mutationsProcessing defectsLaevis oocytes
2010
Mouse cystic fibrosis transmembrane conductance regulator forms cAMP-PKA–regulated apical chloride channels in cortical collecting duct
Lu M, Dong K, Egan ME, Giebisch GH, Boulpaep EL, Hebert SC. Mouse cystic fibrosis transmembrane conductance regulator forms cAMP-PKA–regulated apical chloride channels in cortical collecting duct. Proceedings Of The National Academy Of Sciences Of The United States Of America 2010, 107: 6082-6087. PMID: 20231442, PMCID: PMC2851921, DOI: 10.1073/pnas.0902661107.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBenzoatesChloride ChannelsCyclic AMPCyclic AMP-Dependent Protein KinasesCystic Fibrosis Transmembrane Conductance RegulatorFemaleIn Vitro TechniquesKidney CortexKidney Tubules, CollectingKineticsMiceMice, Inbred C57BLMice, Inbred CFTRMice, KnockoutMice, TransgenicMutationOocytesPatch-Clamp TechniquesPotassium Channels, Inwardly RectifyingRecombinant ProteinsThiazolidinesXenopus laevisConceptsCystic fibrosis transmembrane conductance regulatorFibrosis transmembrane conductance regulatorTransmembrane conductance regulatorCl- channel activityConductance regulatorCl- channelsApical membrane proteinsExpression of CFTRChannel activityCFTR Cl- channelApical chloride channelApical cell membraneDeltaF508 CFTR mutationMembrane proteinsCatalytic subunitXenopus laevis oocytesForm proteinPrincipal cellsCFTR channelsROMK null miceApical patchesApical membraneSingle-channel conductanceChloride channelsCell membrane
2008
A novel missense mutation in SLC34A3 that causes hereditary hypophosphatemic rickets with hypercalciuria in humans identifies threonine 137 as an important determinant of sodium-phosphate cotransport in NaPi-IIc
Jaureguiberry G, Carpenter TO, Forman S, Jüppner H, Bergwitz C. A novel missense mutation in SLC34A3 that causes hereditary hypophosphatemic rickets with hypercalciuria in humans identifies threonine 137 as an important determinant of sodium-phosphate cotransport in NaPi-IIc. American Journal Of Physiology. Renal Physiology 2008, 295: f371-f379. PMID: 18480181, PMCID: PMC2519180, DOI: 10.1152/ajprenal.00090.2008.Peer-Reviewed Original ResearchMeSH KeywordsAdultAllelesAnimalsBase SequenceExocytosisFamilial Hypophosphatemic RicketsFemaleHaplotypesHumansHypercalciuriaKidneyMaleMolecular Sequence DataMutation, MissenseOocytesOpossumsPhosphatesPolymorphism, Single NucleotideSodiumSodium-Phosphate Cotransporter ProteinsSodium-Phosphate Cotransporter Proteins, Type IIcThreonineXenopus laevisConceptsEncoding enhanced green fluorescent proteinHereditary hypophosphatemic ricketsNaPi-IIcSodium-phosphate cotransporterLoss of expressionAmino acid residuesSodium-phosphate cotransportGreen fluorescence proteinImportant functional roleComplete lossOpossum kidneyHypophosphatemic ricketsXenopus laevis oocytesNovel missense mutationPaternal alleleWild-typeFunctional analysisFluorescence proteinNH2 terminusAcid residuesApical patchesCompound heterozygous mutationsExpression plasmidFunctional roleRecurrent kidney stones
2007
Interaction between lysine 102 and aspartate 338 in the insect amino acid cotransporter KAAT1
Castagna M, Soragna A, Mari S, Santacroce M, Betté S, Mandela P, Rudnick G, Peres A, Sacchi V. Interaction between lysine 102 and aspartate 338 in the insect amino acid cotransporter KAAT1. American Journal Of Physiology - Cell Physiology 2007, 293: c1286-c1295. PMID: 17626242, DOI: 10.1152/ajpcell.00190.2007.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAmino Acid SubstitutionAmino Acid Transport Systems, NeutralAnimalsAspartic AcidBinding SitesBiological TransportCross-Linking ReagentsCysteineDithiothreitolFemaleInsect ProteinsKineticsLepidopteraLysineModels, MolecularMolecular Sequence DataOocytesPhenanthrolinesPotassiumProtein Structure, TertiarySequence Homology, Amino AcidSodiumTryptophanXenopus laevisConceptsSingle cysteine mutantsNeutral amino acid transporterSite-directed mutagenesisAmino acid transportersTransport-associated currentNSS transportersDouble mutantXenopus laevis oocytesCysteine mutantsWild typeDependent transportLysine 102MutantsSuper familyAcid transportersPermeation pathwayAmino acidsDisulfide bondsLaevis oocytesFunctional evidenceAsp338Leucine uptakeKAAT1Spatial organizationResidues
2006
Catalytically‐inactive WNK3 bypasses the tonicity requirement for K‐Cl cotransporter activation via a phosphatase‐dependent pathway
De los Heros P, Kahle K, Rinehart J, Bobadilla N, San Cristobal P, Vazquez N, Lifton R, Hebert S, Gamba G. Catalytically‐inactive WNK3 bypasses the tonicity requirement for K‐Cl cotransporter activation via a phosphatase‐dependent pathway. The FASEB Journal 2006, 20: a1224-a1224. DOI: 10.1096/fasebj.20.5.a1224.Peer-Reviewed Original ResearchWNK3, a kinase related to genes mutated in hereditary hypertension with hyperkalaemia, regulates the K+ channel ROMK1 (Kir1.1)
Leng Q, Kahle KT, Rinehart J, MacGregor GG, Wilson FH, Canessa CM, Lifton RP, Hebert SC. WNK3, a kinase related to genes mutated in hereditary hypertension with hyperkalaemia, regulates the K+ channel ROMK1 (Kir1.1). The Journal Of Physiology 2006, 571: 275-286. PMID: 16357011, PMCID: PMC1796803, DOI: 10.1113/jphysiol.2005.102202.Peer-Reviewed Original ResearchConceptsDistal convoluted tubuleInhibition of ROMK1KCNQ1/KCNE1Renal NaCl reabsorptionEpithelial sodium channelAmiloride-sensitive currentDistal nephronVivo effectsConvoluted tubulesKinase-dependent activationQT syndromeNCC activityNaCl reabsorptionNephron segmentsDuct principal cellsHereditary hypertensionSodium channelsPrincipal cellsII cellsRenal NaClSurface expressionXenopus laevis oocytesHypertensionHomeostatic systemDisease
2004
Characteristics of renal Rhbg as an NH4+ transporter
Nakhoul N, DeJong H, Abdulnour-Nakhoul S, Boulpaep E, Hering-Smith K, Hamm L. Characteristics of renal Rhbg as an NH4+ transporter. American Journal Of Physiology. Renal Physiology 2004, 288: f170-f181. PMID: 15353405, DOI: 10.1152/ajprenal.00419.2003.Peer-Reviewed Original Research
2003
WNK4 regulates the balance between renal NaCl reabsorption and K+ secretion
Kahle KT, Wilson FH, Leng Q, Lalioti MD, O'Connell AD, Dong K, Rapson AK, MacGregor GG, Giebisch G, Hebert SC, Lifton RP. WNK4 regulates the balance between renal NaCl reabsorption and K+ secretion. Nature Genetics 2003, 35: 372-376. PMID: 14608358, DOI: 10.1038/ng1271.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCarrier ProteinsClathrinEndocytosisGreen Fluorescent ProteinsIon TransportKidneyLuminescent ProteinsMicePotassiumPotassium ChannelsPotassium Channels, Inwardly RectifyingProtein Serine-Threonine KinasesPseudohypoaldosteronismRatsReceptors, DrugSodium ChlorideSodium Chloride SymportersSolute Carrier Family 12, Member 3SymportersXenopus laevisConceptsDiverse ion transportersClathrin-dependent endocytosisSerine-threonine kinase WNK4WNK4 kinase activityRenal Na-Cl cotransporterDiverse physiologic processesRenal NaClWild-type WNK4Positional cloningMultifunctional regulatorXenopus laevis oocytesInhibition of ROMKIon transportersKinase activityGenetic analysisSystems biologyMolecular switchNa-Cl cotransporterWNK4's inhibitionLaevis oocytesChannel ROMKWNK4Renal NaCl reabsorptionMutationsSame mutation
2002
Functional comparison of renal Na-K-Cl cotransporters between distant species
Gagnon E, Forbush B, Caron L, Isenring P. Functional comparison of renal Na-K-Cl cotransporters between distant species. American Journal Of Physiology - Cell Physiology 2002, 284: c365-c370. PMID: 12388059, DOI: 10.1152/ajpcell.00262.2002.Peer-Reviewed Original ResearchConceptsRenal Na-K-Cl cotransporterNa-K-Cl cotransporterSplice variantsSecond transmembrane domainDistant vertebratesDistant speciesTransmembrane domainAlternative splicingXenopus laevis oocytesTransport activityCl(-) affinityRenal NKCC2Functional comparisonLaevis oocytesSpeciesSharksSimilar affinityIon dependence
2001
α10: A determinant of nicotinic cholinergic receptor function in mammalian vestibular and cochlear mechanosensory hair cells
Elgoyhen A, Vetter D, Katz E, Rothlin C, Heinemann S, Boulter J. α10: A determinant of nicotinic cholinergic receptor function in mammalian vestibular and cochlear mechanosensory hair cells. Proceedings Of The National Academy Of Sciences Of The United States Of America 2001, 98: 3501-3506. PMID: 11248107, PMCID: PMC30682, DOI: 10.1073/pnas.051622798.Peer-Reviewed Original ResearchConceptsHair cellsMechanosensory hair cellsCholinergic receptor functionAgonist-mediated desensitizationHair cell functionAlpha9 nAChREfferent modulationHeteromeric nAChRsAlpha9alpha10 nAChRsPharmacological profileBiphasic responseMammalian vestibularReceptor functionAlpha10 subunitsNAChRsCell functionAlpha9Xenopus laevis oocytesCurrent-voltage relationshipVertebrate hair cellsSubunit geneLaevis oocytesAlpha10CellsAlpha9alpha10
2000
Mixed nicotinic–muscarinic properties of the α9 nicotinic cholinergic receptor
Verbitsky M, Rothlin C, Katz E, Elgoyhen A. Mixed nicotinic–muscarinic properties of the α9 nicotinic cholinergic receptor. Neuropharmacology 2000, 39: 2515-2524. PMID: 11044723, DOI: 10.1016/s0028-3908(00)00124-6.Peer-Reviewed Original ResearchConceptsOuter hair cellsCholinergic receptorsCholinergic compoundsAlpha9 nicotinic acetylcholine receptorHigh ACh concentrationsNicotinic cholinergic receptorsWeak partial agonistNicotinic acetylcholine receptorsCochlear outer hair cellsAgonist-evoked currentsAlpha9 receptorMuscarinic agonistsMaximal responseAcetylcholine receptorsPartial agonistACh concentrationPharmacological propertiesHair cellsReceptorsXenopus laevis oocytesAcetylcholineNative receptorAgonistsCompetitive typeLaevis oocytesBlock of the α9 nicotinic receptor by ototoxic aminoglycosides
Rothlin C, Katz E, Verbitsky M, Vetter D, Heinemann S, Elgoyhen A. Block of the α9 nicotinic receptor by ototoxic aminoglycosides. Neuropharmacology 2000, 39: 2525-2532. PMID: 11044724, DOI: 10.1016/s0028-3908(00)00056-3.Peer-Reviewed Original ResearchConceptsAlpha9 nicotinic acetylcholine receptorConcentration of acetylcholineNicotinic acetylcholine receptorsOrgan of CortiOuter hair cellsConcentration-dependent mannerEfferent functionCholinergic receptorsOtotoxic aminoglycosidesNicotinic receptorsAcetylcholine receptorsNon-competitive typeAcetylcholineHair cellsAminoglycosidesGentamicinXenopus laevis oocytesReceptorsAminoglycoside antibioticsReversible actionAlpha9Rank orderPresent studyAntagonistic effectLaevis oocytesRat homolog of sulfonylurea receptor 2B determines glibenclamide sensitivity of ROMK2 in Xenopus laevisoocyte
Tanemoto M, Vanoye C, Dong K, Welch R, Abe T, Hebert S, Xu J. Rat homolog of sulfonylurea receptor 2B determines glibenclamide sensitivity of ROMK2 in Xenopus laevisoocyte. American Journal Of Physiology. Renal Physiology 2000, 278: f659-f666. PMID: 10751228, DOI: 10.1152/ajprenal.2000.278.4.f659.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsATP-Binding Cassette TransportersFemaleGlyburideKidneyMolecular Sequence DataOocytesPotassium ChannelsPotassium Channels, Inwardly RectifyingProtein IsoformsRatsReceptors, DrugSequence Homology, Amino AcidSulfonylurea ReceptorsTranscription, GeneticXenopus laevisConceptsThick ascending limbAscending limbCortical thick ascending limbRT-PCRMedullary thick ascending limbGlibenclamide sensitivityGlibenclamide effectsRat homologIntrarenal distributionSulfonylurea receptor 2BProximal tubulesDistal distributionSulfonylurea receptorRenal ATPSkeletal muscleRat tissuesXenopus laevis oocytesROMK proteinGlibenclamideRat kidney cDNA librarySUR2BTubulesROMKLimbLaevis oocytesHigh calcium permeability and calcium block of the α9 nicotinic acetylcholine receptor
Katz E, Verbitsky M, Rothlin C, Vetter D, Heinemann S, Elgoyhen A. High calcium permeability and calcium block of the α9 nicotinic acetylcholine receptor. Hearing Research 2000, 141: 117-128. PMID: 10713500, DOI: 10.1016/s0378-5955(99)00214-2.Peer-Reviewed Original ResearchConceptsOuter hair cellsAlpha9 receptorNicotinic acetylcholine receptorsAcetylcholine receptorsAlpha9 nicotinic acetylcholine receptorΑ9 nicotinic acetylcholine receptorHair cellsOlivocochlear efferent fibersHigh calcium permeabilityAuditory nerve fiber activityNerve fiber activityEfferent fibersCholinergic receptorsOlivocochlear fibersVoltage-dependent mannerSynaptic transmissionCalcium permeabilityInhibitory synapseFiber activityReceptorsXenopus laevis oocytesMonovalent currentsLaevis oocytesSynapseCalcium blockResidues of the Fourth Transmembrane Segments of the Na,K-ATPase and the Gastric H,K-ATPase Contribute to Cation Selectivity*
Mense M, Dunbar L, Blostein R, Caplan M. Residues of the Fourth Transmembrane Segments of the Na,K-ATPase and the Gastric H,K-ATPase Contribute to Cation Selectivity*. Journal Of Biological Chemistry 2000, 275: 1749-1756. PMID: 10636871, DOI: 10.1074/jbc.275.3.1749.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphatasesAmino Acid SequenceAnimalsCationsElectrophysiologyH(+)-K(+)-Exchanging ATPaseHydrogen-Ion ConcentrationInhibitory Concentration 50KineticsMolecular Sequence DataMutationOuabainPotassiumRecombinant Fusion ProteinsSequence Homology, Amino AcidSodiumSodium-Potassium-Exchanging ATPaseStomachVanadatesXenopus laevisConceptsFourth transmembrane segmentTransmembrane segmentsATPase assaysK-ATPaseHelical wheel analysisTwo-electrode voltage-clamp experimentsCation selectivityProtein chimerasXenopus laevis oocytesVanadate sensitivityWild-type NaGastric HK-ATPasesXenopus oocytesLaevis oocytesATPase activityAbsence of sodiumResiduesTM4K counterpartsControl constructsOocytesConformational equilibriumAssaysImportant role
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