2011
AMP-activated Protein Kinase (AMPK) Activation and Glycogen Synthase Kinase-3β (GSK-3β) Inhibition Induce Ca2+-independent Deposition of Tight Junction Components at the Plasma Membrane* ♦
Zhang L, Jouret F, Rinehart J, Sfakianos J, Mellman I, Lifton RP, Young LH, Caplan MJ. AMP-activated Protein Kinase (AMPK) Activation and Glycogen Synthase Kinase-3β (GSK-3β) Inhibition Induce Ca2+-independent Deposition of Tight Junction Components at the Plasma Membrane* ♦. Journal Of Biological Chemistry 2011, 286: 16879-16890. PMID: 21383016, PMCID: PMC3089531, DOI: 10.1074/jbc.m110.186932.Peer-Reviewed Original ResearchMeSH KeywordsAMP-Activated Protein KinasesAnimalsCadherinsCalciumCell AdhesionCell MembraneDogsEpitheliumGene Expression Regulation, EnzymologicGlycogen Synthase Kinase 3Glycogen Synthase Kinase 3 betaMembrane ProteinsMicroscopy, FluorescencePhosphoproteinsPhosphorylationRNA InterferenceTight JunctionsZonula Occludens-1 ProteinConceptsProtein kinase activationTight junction componentsJunction componentsPlasma membraneAMPK activationKinase activationGSK-3β inhibitionNectin-afadin systemEpithelial tight junctionsTight junctionsPhosphorylation studiesSynthase kinaseJunctional proteinsAbsence of extracellularDistinct pathwaysCell growthE-cadherinIndependent depositionKinaseActivationInduce Ca2MembraneAfadinExtracellularInhibition
2010
Association with β-COP Regulates the Trafficking of the Newly Synthesized Na,K-ATPase*
Morton MJ, Farr GA, Hull M, Capendeguy O, Horisberger JD, Caplan MJ. Association with β-COP Regulates the Trafficking of the Newly Synthesized Na,K-ATPase*. Journal Of Biological Chemistry 2010, 285: 33737-33746. PMID: 20801885, PMCID: PMC2962472, DOI: 10.1074/jbc.m110.141119.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCell MembraneChlorocebus aethiopsCoatomer ProteinCOS CellsDogsEndoplasmic ReticulumEpitopesGene Expression Regulation, EnzymologicGolgi ApparatusMutationProtein BindingRatsSodium-Potassium-Exchanging ATPaseConceptsK-ATPase αK-ATPase β-subunitΒ-COPΒ-subunitΑ-subunitPlasma membraneEndoplasmic reticulumK-ATPase α-subunitMutant α-subunitsIon-transporting ATPasePlasma membrane expressionK-ATPasePulse-chase experimentsPartner proteinsNovel labeling techniqueCoat proteinDibasic motifCell surfaceMembrane expressionObligate intermediateΒ subunit expressionProteinReticulum
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 ResearchMeSH KeywordsAnimalsCell PolarityEpithelial CellsFluorescent Antibody TechniqueGene Expression Regulation, EnzymologicH(+)-K(+)-Exchanging ATPaseHumansKidneyLLC-PK1 CellsMicroscopy, ConfocalStomachSwineTransfectionConceptsApical 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 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 lossATPaseAssemblyExpressionSubunits