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
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 2Endosomes
1998
Gastric 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 Research
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
1994
Chapter 8 Synthesis and Sorting of Ion Pumps in Polarized Cells
Gottardi C, Pietrini G, Shiel M, Caplan M. Chapter 8 Synthesis and Sorting of Ion Pumps in Polarized Cells. Current Topics In Membranes 1994, 41: 143-168. DOI: 10.1016/s0070-2161(08)60458-x.Peer-Reviewed Original ResearchDistinct biochemical compositionsCellular polarityIntercellular junctional complexesPolarized cellsTertiary structureCellular componentsBiologic contextCell typesTerm polarityJunctional complexesIon pumpsBiochemical compositionProteinAppropriate localizationMachineryDistinguishable domainsSeparate body compartmentsFunctional propertiesCellsPolarityPlasmalemmaSortingCompartmentsMembraneEvidence of polarity
1987
Processing and Sorting of Proteins Synthesized in the Endoplasmic Reticulum
Caplan M, Rosenzweig S, Jamieson J. Processing and Sorting of Proteins Synthesized in the Endoplasmic Reticulum. 1987, 273-281. DOI: 10.1007/978-1-4613-1943-6_16.Peer-Reviewed Original ResearchIntracellular membrane-bounded compartmentsEndoplasmic reticulumSorting of proteinsRough endoplasmic reticulumMembrane-bounded compartmentsIntracellular digestion processSpecialized functional domainsEukaryotic cellsMembrane proteinsFunctional domainsSecretory proteinsIntracellular compartmentsLysosomal hydrolasesProteinExtracellular spaceMajor classesReticulumCompartmentsBiogenesisCommon setCellsHydrolasesPlasmalemmaDigestion processSorting
1986
Processing and Sorting of Proteins Synthesized in the Endoplasmic Reticulum
Caplan M, Rosenzweig S, Jamieson J. Processing and Sorting of Proteins Synthesized in the Endoplasmic Reticulum. 1986, 273-281. DOI: 10.1007/978-1-4613-2097-5_16.Peer-Reviewed Original ResearchIntracellular membrane-bounded compartmentsEndoplasmic reticulumSorting of proteinsRough endoplasmic reticulumMembrane-bounded compartmentsIntracellular digestion processSpecialized functional domainsEukaryotic cellsMembrane proteinsFunctional domainsSecretory proteinsIntracellular compartmentsLysosomal hydrolasesProteinExtracellular spaceMajor classesReticulumCompartmentsBiogenesisCommon setCellsHydrolasesPlasmalemmaDigestion processSorting