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
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
1987
Dependence on pH of polarized sorting of secreted proteins
Caplan M, Stow J, Newman A, Madri J, Anderson H, Farquhar M, Palade G, Jamieson J. Dependence on pH of polarized sorting of secreted proteins. Nature 1987, 329: 632-635. PMID: 2821405, DOI: 10.1038/329632a0.Peer-Reviewed Original ResearchConceptsSecretory proteinsMDCK cellsDifferent protein compositionsBasolateral cell surfacePolarized sortingMembrane proteinsBasolateral domainDefault pathwayPlasma membraneAcidic intracellular compartmentsIntracellular compartmentsProtein compositionMembrane componentsCell surfaceBasement membrane componentsProteinSecrete lamininDistinct setsRenal tubule cellsEpithelial cellsActive sortingBasolateral compartmentCellsSecretory productsSpecific regionsProcessing 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