2007
Tetraspan proteins: regulators of renal structure and function
Caplan MJ, Kamsteeg EJ, Duffield A. Tetraspan proteins: regulators of renal structure and function. Current Opinion In Nephrology & Hypertension 2007, 16: 353-358. PMID: 17565278, DOI: 10.1097/mnh.0b013e328177b1fa.Peer-Reviewed Original ResearchConceptsProtein partnersRenal ion transport proteinsIon transport proteinsModulates cell adhesionImportant physiological ramificationsNormal glomerular architecturePartner proteinsTissue morphogenesisMembrane proteinsEndocytic internalizationTransport proteinsPhysiological processesRegulatory rolePhysiological ramificationsTransporter functionCell adhesionIntegrin moleculesTetraspan familyProteinEpithelial cellsTetraspansGlomerular architectureNovel classFunctional propertiesCellsThe Future of the Pump
Caplan MJ. The Future of the Pump. Journal Of Clinical Gastroenterology 2007, 41: s217-s222. PMID: 17575526, DOI: 10.1097/mcg.0b013e31803233da.Peer-Reviewed Original ResearchConceptsIon transport proteinsLarge macromolecular complexesMacromolecular complexesGastric parietal cellsTransport proteinsSecond messengerMacromolecular interactionsIon translocationRegulatory processesK-ATPaseCritical roleTight controlX-ray crystallographic techniquesParietal cellsCrystallographic techniquesCellsKinasePharmacologic suppressionTraffickingProteinTranslocationMessengerMolecular structureRegulationSecretion
2006
An Extracellular Loop of the Human Non-Gastric H,K-ATPase a-subunit is Involved in Apical Plasma Membrane Polarization
Lerner M, Lemke D, Bertram H, Schillers H, Oberleithner H, Caplan MJ, Reinhardt J. An Extracellular Loop of the Human Non-Gastric H,K-ATPase a-subunit is Involved in Apical Plasma Membrane Polarization. Cellular Physiology And Biochemistry 2006, 18: 75-84. PMID: 16914892, DOI: 10.1159/000095169.Peer-Reviewed Original ResearchConceptsP-type ATPasesSorting motifApical deliveryExtracellular loopK-ATPaseSpecific sorting signalsPlasma membrane polarizationShort extracellular loopApical plasma membraneMadin-Darby canine kidney cellsSingle point mutationCanine kidney cellsSorting signalsGene familyPlasma membraneFlanking regionsEpithelial apical membraneK-ATPasesPhysiological roleApical membraneCellular distributionPoint mutationsIon pumpsATP1AL1Corresponding region
2004
Sorting of H,K‐ATPase β‐Subunit in MDCK and LLC‐PK1 Cells is Independent of μ1B Adaptin Expression
Duffield A, Fölsch H, Mellman I, Caplan MJ. Sorting of H,K‐ATPase β‐Subunit in MDCK and LLC‐PK1 Cells is Independent of μ1B Adaptin Expression. Traffic 2004, 5: 449-461. PMID: 15117319, DOI: 10.1111/j.1398-9219.2004.00192.x.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Protein Complex mu SubunitsAdaptor Proteins, Vesicular TransportAmino Acid MotifsAnimalsCell LineCytoplasmDogsEpithelial CellsGlutathione TransferaseH(+)-K(+)-Exchanging ATPaseLLC-PK1 CellsMembrane ProteinsProtein SubunitsProtein TransportReceptors, LDLReceptors, TransferrinRecombinant Fusion ProteinsSwineTransfectionTyrosineConceptsLow-density lipoproteinTransferrin receptorBasolateral localizationTyrosine-based motifMDCK cellsB expressionLLC-PK1 cellsEpithelial cellsLipoproteinMadin-Darby canine kidney cellsCertain epithelial cellsReceptorsKidney cellsCanine kidney cellsK-ATPase beta subunitCellsDifferential expressionK-ATPaseBasolateral expressionExpressionApical membrane
2003
The tetraspanin CD63 enhances the internalization of the H,K-ATPase β-subunit
Duffield A, Kamsteeg EJ, Brown AN, Pagel P, Caplan MJ. The tetraspanin CD63 enhances the internalization of the H,K-ATPase β-subunit. Proceedings Of The National Academy Of Sciences Of The United States Of America 2003, 100: 15560-15565. PMID: 14660791, PMCID: PMC307607, DOI: 10.1073/pnas.2536699100.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAntigens, CDChlorocebus aethiopsCloning, MolecularCOS CellsGene LibraryH(+)-K(+)-Exchanging ATPaseHumansKidneyMembrane ProteinsModels, BiologicalPlatelet Membrane GlycoproteinsProtein SubunitsProtein TransportRabbitsRatsRats, Sprague-DawleyRecombinant ProteinsTetraspanin 30TransfectionConceptsAdaptor protein complex 2Intracellular compartmentsK-ATPaseTetraspanin CD63K-ATPase β-subunitCOS-7 cellsEndocytic machineryAdaptor proteinLate endosomesSecretory vesiclesPlasma membraneGastric parietal cellsBiochemical experimentsInteraction partnersΒ-subunitParietal cellsCell surfaceEnhanced endocytosisTubulovesicular elementsCD63CompartmentsCellsInternalizationComplexes 2EndosomesIon Pump‐Interacting Proteins: Promising New Partners
PAGEL P, ZATTI A, KIMURA T, DUFFIELD A, CHAUVET V, RAJENDRAN V, CAPLAN MJ. Ion Pump‐Interacting Proteins: Promising New Partners. Annals Of The New York Academy Of Sciences 2003, 986: 360-368. PMID: 12763851, DOI: 10.1111/j.1749-6632.2003.tb07215.x.Peer-Reviewed Original Research
2002
Extracellular Domains, Transmembrane Segments, and Intracellular Domains Interact To Determine the Cation Selectivity of Na,K- and Gastric H,K-ATPase †
Mense M, Rajendran V, Blostein R, Caplan MJ. Extracellular Domains, Transmembrane Segments, and Intracellular Domains Interact To Determine the Cation Selectivity of Na,K- and Gastric H,K-ATPase †. Biochemistry 2002, 41: 9803-9812. PMID: 12146946, DOI: 10.1021/bi025819z.Peer-Reviewed Original Research
2001
Ion Pumps in Polarized Cells: Sorting and Regulation of the Na+,K+- and H+,K+-ATPases*
Dunbar L, Caplan M. Ion Pumps in Polarized Cells: Sorting and Regulation of the Na+,K+- and H+,K+-ATPases*. Journal Of Biological Chemistry 2001, 276: 29617-29620. PMID: 11404365, DOI: 10.1074/jbc.r100023200.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsGene Expression Regulation, EnzymologicH(+)-K(+)-Exchanging ATPaseHumansIonsModels, MolecularProtein BindingSignal TransductionSodium-Potassium-Exchanging ATPaseConceptsP-type familyIon transport proteinsDistinct regulatory pathwaysSubcellular localizationPolarized cellsRelated membersRegulatory pathwaysTransport proteinsMolecular signalsATPasesCellular mechanismsIon pumpsEnzymatic activityEpithelial cellsProteinComplex arrayCatalytic capacityPhysiologic functionIntramolecular interactionsCellsHomologyTraffickingATPasePathwayRegulation
2000
Differential localization of human nongastric H+-K+-ATPase ATP1AL1 in polarized renal epithelial cells
Reinhardt J, Grishin A, Oberleithner H, Caplan M. Differential localization of human nongastric H+-K+-ATPase ATP1AL1 in polarized renal epithelial cells. American Journal Of Physiology. Renal Physiology 2000, 279: f417-f425. PMID: 10966921, DOI: 10.1152/ajprenal.2000.279.3.f417.Peer-Reviewed Original ResearchConceptsApical plasma membranePlasma membraneRenal epithelial cellsIon pumpsPlasma membrane localizationConfocal immunofluorescence microscopyEpithelial cellsATPase beta subunitRenal epithelial cell lineMembrane localizationLow expression levelsEpithelial cell lineSurface biotinylationPump subunitsBeta subunitFunctional expressionStable transfectionLateral membranesMDCK cellsATP1AL1Immunofluorescence microscopyDifferential localizationSorting mechanismStable interactionExpression levelsThe cell biology of ion pumps: sorting and regulation
Dunbar L, Caplan M. The cell biology of ion pumps: sorting and regulation. European Journal Of Cell Biology 2000, 79: 557-563. PMID: 11001492, DOI: 10.1078/0171-9335-00079.Peer-Reviewed Original ResearchConceptsPolarized epithelial cellsP-type familyIon pumpsK-ATPaseDistinct regulatory pathwaysProtein traffickingSubcellular localizationCell biologyRelated membersRegulatory pathwaysMolecular signalsCellular mechanismsEnzymatic activityIntra-molecular interactionsEpithelial cellsTraffickingComplex arrayCatalytic capacityPhysiologic functionATPasesHomologyBiologyPathwayRegulationSortingThe Roles of Carbohydrate Chains of the β-Subunit on the Functional Expression of Gastric H+,K+-ATPase*
Asano S, Kawada K, Kimura T, Grishin A, Caplan M, Takeguchi N. The Roles of Carbohydrate Chains of the β-Subunit on the Functional Expression of Gastric H+,K+-ATPase*. Journal Of Biological Chemistry 2000, 275: 8324-8330. PMID: 10722662, DOI: 10.1074/jbc.275.12.8324.Peer-Reviewed Original ResearchConceptsAlpha/beta assemblyN-glycosylation sitesATPase activityBeta assemblyPutative N-glycosylation sitesCarbohydrate chainsAlpha/beta complexSingle carbohydrate chainCatalytic subunitSurface deliveryFunctional enzymeAsparagine residuesAlpha subunitΒ-subunitBeta complexDelivery mechanismFunctional expressionComplete lossATPaseAssemblyExpressionSubunitsA Transmembrane Segment Determines the Steady-State Localization of an Ion-Transporting Adenosine Triphosphatase
Dunbar L, Aronson P, Caplan M. A Transmembrane Segment Determines the Steady-State Localization of an Ion-Transporting Adenosine Triphosphatase. Journal Of Cell Biology 2000, 148: 769-778. PMID: 10684257, PMCID: PMC2169368, DOI: 10.1083/jcb.148.4.769.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBiological TransportCationsCell LineCell MembraneCell PolarityGlycosphingolipidsGlycosylphosphatidylinositolsH(+)-K(+)-Exchanging ATPaseHydrogen-Ion ConcentrationMembrane ProteinsMolecular Sequence DataOuabainParietal Cells, GastricProtein Sorting SignalsRecombinant Fusion ProteinsSequence AlignmentSequence DeletionSodium-Potassium-Exchanging ATPaseSolubilityTransfectionConceptsK-ATPase alpha subunitAlpha subunitTransmembrane domainPolytopic membrane transport proteinK-ATPaseApical distributionGlycosphingolipid-rich membrane domainsDetergent-insoluble complexesMembrane transport proteinsApical membrane proteinsApical plasma membraneK-ATPase alphaFourth transmembrane domainLocalization signalChimeric pumpsFourth transmembraneTransmembrane segmentsK-ATPase sequencesMembrane compartmentsMembrane domainsMembrane proteinsSequence domainsPlasma membraneGastric parietal cellsTransport proteinsResidues 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
1999
Nongastric H+,K+-ATPase: cell biologic and functional properties.
Grishin AV, Reinhard J, Dunbar LA, Courtois-Coutry N, Wang T, Giebisch G, Caplan MJ. Nongastric H+,K+-ATPase: cell biologic and functional properties. Seminars In Nephrology 1999, 19: 421-30. PMID: 10511382.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCells, CulturedH(+)-K(+)-Exchanging ATPaseHumansIon TransportKidney Tubules, CollectingMiceMice, TransgenicStomachUrotheliumWater-Electrolyte BalanceConceptsATPase isoformsP-type ATPasesEndocytic regulationEndocytosis signalATPase familyCell machineryCytoplasmic tailK resorptionATPasesIon pumpsATPase isoform expressionApical surfaceIsoformsCell biologicIsoform expressionPhysiological studiesTubule epithelial cellsATPaseEpithelial cellsTransgenic miceCation transportK transportFunctional propertiesRenal K transportEndocytosisCation Selectivity of Gastric H,K-ATPase and Na,K-ATPase Chimeras*
Blostein R, Dunbar L, Mense M, Scanzano R, Wilczynska A, Caplan M. Cation Selectivity of Gastric H,K-ATPase and Na,K-ATPase Chimeras*. Journal Of Biological Chemistry 1999, 274: 18374-18381. PMID: 10373442, DOI: 10.1074/jbc.274.26.18374.Peer-Reviewed Original Research
1998
A tyrosine-based signal regulates H-K-ATPase-mediated potassium reabsorption in the kidney
Wang T, Courtois-Coutry N, Giebisch G, Caplan M. A tyrosine-based signal regulates H-K-ATPase-mediated potassium reabsorption in the kidney. American Journal Of Physiology 1998, 275: f818-f826. PMID: 9815140, DOI: 10.1152/ajprenal.1998.275.5.f818.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsH(+)-K(+)-Exchanging ATPaseKidney Tubules, CollectingMaleMiceMice, Inbred C57BLMice, TransgenicPotassiumSignal TransductionTyrosineConceptsGlomerular filtration rateTransgenic miceGastric acid outputPlasma K concentrationK pumpK-ATPaseRenal collecting tubulesK clearanceBlood pressurePotassium reabsorptionAcid outputUrine volumeK excretionFiltration rateGastric acidK reabsorptionPump functionCollecting tubuleMicePlasma NaTyrosine-based sequenceTyrosine-based signalsKidneyExcretionCytoplasmic tailTyrosine-based Membrane Protein Sorting Signals Are Differentially Interpreted by Polarized Madin-Darby Canine Kidney and LLC-PK1 Epithelial Cells*
Roush D, Gottardi C, Naim H, Roth M, Caplan M. Tyrosine-based Membrane Protein Sorting Signals Are Differentially Interpreted by Polarized Madin-Darby Canine Kidney and LLC-PK1 Epithelial Cells*. Journal Of Biological Chemistry 1998, 273: 26862-26869. PMID: 9756932, DOI: 10.1074/jbc.273.41.26862.Peer-Reviewed Original ResearchConceptsProtein sorting signalsTyrosine-based motifLLC-PK1 cellsCytoplasmic tailSorting signalsMDCK cellsApical membraneBeta-subunit polypeptidesBasolateral membraneK-ATPase beta subunitDi-leucine motifBeta subunit proteinLLC-PK1 epithelial cellsMadin-Darby canine kidney cellsMadin-Darby canine kidneyEpithelial cell typesCanine kidney cellsK-ATPase betaHA-Y543Cytoplasmic sequencesSequence motifsSubunit polypeptidesMembrane proteinsBasolateral domainPolarized epitheliumATP1AL1, a Member of the Non-gastric H,K-ATPase Family, Functions as a Sodium Pump*
Grishin A, Caplan M. ATP1AL1, a Member of the Non-gastric H,K-ATPase Family, Functions as a Sodium Pump*. Journal Of Biological Chemistry 1998, 273: 27772-27778. PMID: 9774385, DOI: 10.1074/jbc.273.43.27772.Peer-Reviewed Original ResearchGastric H+/K+-ATPase: targeting signals in the regulation of physiologic function
Caplan M. Gastric H+/K+-ATPase: targeting signals in the regulation of physiologic function. Current Opinion In Cell Biology 1998, 10: 468-473. PMID: 9719867, DOI: 10.1016/s0955-0674(98)80060-4.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsGastric AcidH(+)-K(+)-Exchanging ATPaseHumansIon PumpsSignal TransductionStomachSorting of P-type ATPases in polarized epithelial cells.
Dunbar LA, Courtois-Coutry N, Roush DL, Muth TR, Gottardi CJ, Rajendran V, Geibel J, Kashgarian M, Caplan MJ. Sorting of P-type ATPases in polarized epithelial cells. Acta Physiologica Scandinavica. Supplementum 1998, 643: 289-95. PMID: 9789572.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCell PolarityEpithelial CellsH(+)-K(+)-Exchanging ATPaseSodium-Potassium-Exchanging ATPaseConceptsApical localizationK-ATPaseMost epithelial cell typesTyrosine-based signalsP-type familyP-type ATPasesEpithelial cellsCritical tyrosine residuesApical plasma membraneFourth transmembrane domainBeta-subunit sequencesApical cell surfaceEpithelial cell typesSorting signalsTransmembrane domainCytoplasmic tailSequence domainsPlasma membraneHomologous membersTyrosine residuesParietal cellsStorage compartmentCell typesCell surfaceBasolateral surface