2009
POSH Stimulates the Ubiquitination and the Clathrin-independent Endocytosis of ROMK1 Channels*
Lin DH, Yue P, Pan CY, Sun P, Zhang X, Han Z, Roos M, Caplan M, Giebisch G, Wang WH. POSH Stimulates the Ubiquitination and the Clathrin-independent Endocytosis of ROMK1 Channels*. Journal Of Biological Chemistry 2009, 284: 29614-29624. PMID: 19710010, PMCID: PMC2785594, DOI: 10.1074/jbc.m109.041582.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingAnimalsBiological TransportCell LineClathrinDynaminsEpithelial Sodium ChannelsGene Expression RegulationHumansKidney Tubules, CollectingOocytesPotassium Channels, Inwardly RectifyingProtein Sorting SignalsProtein Structure, TertiaryRatsRats, Sprague-DawleyUbiquitinationUbiquitin-Protein LigasesXenopus laevisConceptsHEK293T cellsClathrin-independent endocytosisE3 ubiquitin ligaseUbiquitin ligaseGlutathione S-transferase pulldown experimentsROMK1 channelsT cellsTyrosine-based internalization signalPotassium currentROMK channelsDominant-negative dynaminImmunoprecipitation of lysatesInternalization signalInhibitory effectPulldown experimentsScaffold proteinUbiquitination assaysRING domainUbiquitinationN-terminusGamma subunitsAmino acidsENaC-alphaROMK1Tissue lysates
2008
Expression of Tetraspan Protein CD63 Activates Protein-tyrosine Kinase (PTK) and Enhances the PTK-induced Inhibition of ROMK Channels*
Lin D, Kamsteeg EJ, Zhang Y, Jin Y, Sterling H, Yue P, Roos M, Duffield A, Spencer J, Caplan M, Wang WH. Expression of Tetraspan Protein CD63 Activates Protein-tyrosine Kinase (PTK) and Enhances the PTK-induced Inhibition of ROMK Channels*. Journal Of Biological Chemistry 2008, 283: 7674-7681. PMID: 18211905, DOI: 10.1074/jbc.m705574200.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAntigens, CDBenzoquinonesCSK Tyrosine-Protein KinaseEnzyme InhibitorsFemaleGene Expression RegulationHumansKidney CortexKidney MedullaLactams, MacrocyclicMaleOocytesOrgan SpecificityPatch-Clamp TechniquesPhosphorylationPlatelet Membrane GlycoproteinsPotassium Channels, Inwardly RectifyingProtein-Tyrosine KinasesProto-Oncogene ProteinsRatsRats, Sprague-DawleyReceptor-Like Protein Tyrosine Phosphatases, Class 4RifabutinSrc-Family KinasesTetraspanin 30TransfectionXenopus laevisConceptsExpression of CD63T cellsOuter medullaRenal cortexROMK channelsProtein tyrosine kinasesC-SrcRole of CD63Potassium restrictionROMK activityPotassium currentTwo-electrode voltage clampRat kidneyDecreased expressionImmunocytochemical stainingROMK1 channelsInhibitory effectMedullaNative rat kidneyCD63Voltage clampCortexRPTPalphaTyrosine phosphorylationHerbimycin A
2006
CFTR is required for PKA-regulated ATP sensitivity of Kir1.1 potassium channels in mouse kidney
Lu M, Leng Q, Egan ME, Caplan MJ, Boulpaep EL, Giebisch GH, Hebert SC. CFTR is required for PKA-regulated ATP sensitivity of Kir1.1 potassium channels in mouse kidney. Journal Of Clinical Investigation 2006, 116: 797-807. PMID: 16470247, PMCID: PMC1361349, DOI: 10.1172/jci26961.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAnimalsCurcuminCyclic AMP-Dependent Protein KinasesCystic Fibrosis Transmembrane Conductance RegulatorHydrogen-Ion ConcentrationKidneyMiceMice, Inbred C57BLMice, Inbred CFTRMice, TransgenicMutationOocytesPatch-Clamp TechniquesPotassium Channels, Inwardly RectifyingXenopus laevisConceptsFunctional switchCystic fibrosis transmembrane conductance regulator (CFTR) Cl(-) channelATP sensitivityEffects of CFTRThick ascending limbPotential physiological rolePKA activityRenal K channelsCystic fibrosisPhysiological roleSecretory channelsK channelsRenal tubule epithelial cellsApical membraneCFTRDeltaF508 mutationDistal nephron segmentsCl- channelsK homeostasisTubule epithelial cellsEpithelial cellsTAL cellsPotassium channelsK handlingGlibenclamide sensitivity
2000
Residues 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