2015
Akt Substrate of 160 kD Regulates Na+,K+-ATPase Trafficking in Response to Energy Depletion and Renal Ischemia
Alves DS, Thulin G, Loffing J, Kashgarian M, Caplan MJ. Akt Substrate of 160 kD Regulates Na+,K+-ATPase Trafficking in Response to Energy Depletion and Renal Ischemia. Journal Of The American Society Of Nephrology 2015, 26: 2765-2776. PMID: 25788531, PMCID: PMC4625659, DOI: 10.1681/asn.2013101040.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBiotinylationCell LineCytoplasmDogsDynaminsEndocytosisEpithelial CellsGTPase-Activating ProteinsHumansIschemiaKidneyKidney DiseasesMadin Darby Canine Kidney CellsMaleMiceMice, KnockoutMicroscopy, FluorescencePhosphorylationProtein TransportReperfusion InjuryRNA, Small InterferingSignal TransductionSodium-Potassium-Exchanging ATPaseConceptsRenal epithelial cellsATPase traffickingIntracellular compartmentsEpithelial cell polarityEpithelial cellsBasolateral plasma membraneGlucose transporter 4Cultured epithelial cellsCell polarityRab GTPaseAkt substratePlasma membraneSubcellular distributionAS160Energy depletionDirect bindingTransporter 4TraffickingDirect roleK-ATPaseATPaseTubular soluteIntracellular accumulationCellsCompartments
2010
AS160 Associates with the Na+,K+-ATPase and Mediates the Adenosine Monophosphate-stimulated Protein Kinase-dependent Regulation of Sodium Pump Surface Expression
Alves DS, Farr GA, Seo-Mayer P, Caplan MJ. AS160 Associates with the Na+,K+-ATPase and Mediates the Adenosine Monophosphate-stimulated Protein Kinase-dependent Regulation of Sodium Pump Surface Expression. Molecular Biology Of The Cell 2010, 21: 4400-4408. PMID: 20943949, PMCID: PMC3002392, DOI: 10.1091/mbc.e10-06-0507.Peer-Reviewed Original ResearchMeSH KeywordsAMP-Activated Protein KinasesAnimalsBiological TransportCell LineChlorocebus aethiopsCOS CellsDogsDose-Response Relationship, DrugEndocytosisEpithelial CellsGene ExpressionGene Knockdown TechniquesGTPase-Activating ProteinsHumansImmunoprecipitationPhosphorylationPyrazolesPyrimidinesSignal TransductionSodium-Potassium-Exchanging ATPaseConceptsRab-GTPase-activating proteinMost epithelial cell typesCompound CProtein kinase‐dependent regulationKinase-dependent regulationActive transport proteinsMadin-Darby canine kidneyEpithelial cell typesRegulated endocytosisShort hairpin RNASurface expressionATPase endocytosisCell surface expressionProtein kinasePlasma membraneCOS cellsTransport proteinsΑ-subunitHairpin RNAAS160Cell typesIntracellular retentionVariety of mechanismsATPaseATPase activityMAL/VIP17, a New Player in the Regulation of NKCC2 in the Kidney
Carmosino M, Rizzo F, Procino G, Basco D, Valenti G, Forbush B, Schaeren-Wiemers N, Caplan MJ, Svelto M. MAL/VIP17, a New Player in the Regulation of NKCC2 in the Kidney. Molecular Biology Of The Cell 2010, 21: 3985-3997. PMID: 20861303, PMCID: PMC2982131, DOI: 10.1091/mbc.e10-05-0456.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBlotting, WesternCell LineEndocytosisEpithelial CellsHumansImmunoprecipitationKidneyLLC-PK1 CellsMembrane Transport ProteinsMiceMice, TransgenicMyelin and Lymphocyte-Associated Proteolipid ProteinsMyelin ProteinsPhosphorylationProtein BindingProteolipidsRatsRats, Inbred WKYRNA InterferenceSodium-Potassium-Chloride SymportersSolute Carrier Family 12, Member 1SwineConceptsRegulation of NKCC2Apical membraneMajor salt transport pathwayC-terminal tailCell surface retentionApical sortingPorcine kidney cellsCotransporter phosphorylationTransgenic mice resultsNephron structuresRegulated absorptionImportant roleNew playersKidney cellsSurface expressionMice resultsSurface retentionTransport pathwaysNKCC2MembraneRegulationLymphocyte-associated proteinCyst formationRat kidney medullaColocalize
2004
Gastric parietal cell acid secretion in mice can be regulated independently of H+/K+ ATPase endocytosis
Nguyen NV, Gleeson PA, Courtois-Coutry N, Caplan MJ, van Driel IR. Gastric parietal cell acid secretion in mice can be regulated independently of H+/K+ ATPase endocytosis. Gastroenterology 2004, 127: 145-154. PMID: 15236181, DOI: 10.1053/j.gastro.2004.04.016.Peer-Reviewed Original ResearchConceptsApical plasma membranePlasma membraneIntracellular traffickingTyrosine-based endocytosis motifATPase activityATPase beta subunitMembrane traffickingATPase endocytosisTrafficking eventsEndocytosis motifParietal cell ultrastructureTubulovesicular compartmentCytoplasmic tailIntracytoplasmic compartmentCl- conductanceParietal cell acid secretionBeta subunitParietal cellsDirect regulationProton pumpCell ultrastructureTraffickingATPaseCellsRegulation
2002
Aquaporin-2: COOH terminus is necessary but not sufficient for routing to the apical membrane
Deen PM, Van Balkom BW, Savelkoul PJ, Kamsteeg EJ, Van Raak M, Jennings ML, Muth TR, Rajendran V, Caplan MJ. Aquaporin-2: COOH terminus is necessary but not sufficient for routing to the apical membrane. American Journal Of Physiology. Renal Physiology 2002, 282: f330-f340. PMID: 11788448, DOI: 10.1152/ajprenal.0168.2001.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAquaporin 1Aquaporin 2Aquaporin 6AquaporinsArginine VasopressinBlood Group AntigensCell CompartmentationCell FractionationCell LineCell MembraneCell Membrane PermeabilityColforsinEndocytosisGene ExpressionHumansKidneyProtein Structure, TertiaryProtein TransportRatsRecombinant Fusion ProteinsVasoconstrictor AgentsWaterConceptsIntracellular vesiclesApical membraneAquaporin-2Wild‐type aquaporin‐2Mammalian water homeostasisMadin-Darby canine kidney cellsCanine kidney cellsAQP2 accumulationPrimary sequenceSame proteinOsmotic water permeabilityApical expressionForskolin treatmentAquaporin-1 (AQP1) water channelWater homeostasisKidney cellsBasolateral membraneVesiclesPlacental alkaline phosphataseMembraneWater channelsDuct cellsAQP1TailCells
2000
The C-terminal Tail of the Metabotropic Glutamate Receptor Subtype 7 Is Necessary but Not Sufficient for Cell Surface Delivery and Polarized Targeting in Neurons and Epithelia*
McCarthy J, Lim S, Elkind N, Trimmer J, Duvoisin R, Rodriguez-Boulan E, Caplan M. The C-terminal Tail of the Metabotropic Glutamate Receptor Subtype 7 Is Necessary but Not Sufficient for Cell Surface Delivery and Polarized Targeting in Neurons and Epithelia*. Journal Of Biological Chemistry 2000, 276: 9133-9140. PMID: 11106656, DOI: 10.1074/jbc.m008290200.Peer-Reviewed Original ResearchConceptsPolarized targetingCytoplasmic tailIntracellular compartmentsMadin-Darby canine kidney epithelial cellsVesicular stomatitis virus G proteinComplex neuronal functionMDCK cellsCell surface deliveryC-terminal tailCanine kidney epithelial cellsCytoplasmic tail domainVirus G proteinKidney epithelial cellsEntire cell surfaceCell surface expressionCytoplasmic domainTransmembrane portionSurface deliveryTail domainSynaptic microdomainsHuman placental alkaline phosphataseNeuronal polarizationMolecular signalsG proteinsCultured hippocampal neurons
1998
Tyrosine-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 epithelium
1997
A Tyrosine-Based Signal Targets H/K-ATPase to a Regulated Compartment and Is Required for the Cessation of Gastric Acid Secretion
Courtois-Coutry N, Roush D, Rajendran V, McCarthy J, Geibel J, Kashgarian M, Caplan M. A Tyrosine-Based Signal Targets H/K-ATPase to a Regulated Compartment and Is Required for the Cessation of Gastric Acid Secretion. Cell 1997, 90: 501-510. PMID: 9267030, DOI: 10.1016/s0092-8674(00)80510-3.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCalciumCOS CellsCytomegalovirusDNA PrimersEndocytosisGastric AcidGastric MucosaH(+)-K(+)-Exchanging ATPaseMacromolecular SubstancesMiceMice, TransgenicMicroscopy, ImmunoelectronMutagenesis, Site-DirectedParietal Cells, GastricPolymerase Chain ReactionPromoter Regions, GeneticRecombinant ProteinsSignal TransductionTransfectionTyrosineConceptsK-ATPase beta subunitTyrosine-based signalsK-ATPaseTyrosine-based endocytosis signalTyrosine residuesBeta subunitIntracellular storage compartmentEndocytosis signalCytoplasmic tailMutant betaRegulated compartmentsSecrete acidResidue sequenceStorage compartmentCell surfaceCell plasmalemmaSubunitsTransgenic miceParietal cellsGastric glandsCompartmentsSecretionAcid secretionReinternalizationPlasmalemma
1993
An ion-transporting ATPase encodes multiple apical localization signals.
Gottardi CJ, Caplan MJ. An ion-transporting ATPase encodes multiple apical localization signals. Journal Of Cell Biology 1993, 121: 283-293. PMID: 8385670, PMCID: PMC2200096, DOI: 10.1083/jcb.121.2.283.Peer-Reviewed Original ResearchConceptsK-ATPaseIon-transporting ATPaseDifferential subcellular distributionEpithelial cell typesEpithelial sortingEpithelial cellsEndocytosis signalLocalization signalEndocytic pathwayMembrane proteinsPlasmalemmal domainsApical localizationMolecular signalsSubcellular distributionBeta subunitRenal proximal tubular epithelial cellsCell typesIon pumpsApical surfaceDistinct populationsFull lengthBasolateral membraneProximal tubular epithelial cellsIndependent signalsTubular epithelial cells