2015
Dual pulse-chase microscopy reveals early divergence in the biosynthetic trafficking of the Na,K-ATPase and E-cadherin
Farr GA, Hull M, Stoops EH, Bateson R, Caplan MJ. Dual pulse-chase microscopy reveals early divergence in the biosynthetic trafficking of the Na,K-ATPase and E-cadherin. Molecular Biology Of The Cell 2015, 26: 4401-4411. PMID: 26424804, PMCID: PMC4666135, DOI: 10.1091/mbc.e14-09-1385.Peer-Reviewed Original ResearchConceptsTrans-Golgi networkPlasma membraneE-cadherinK-ATPasePolarized MDCK epithelial cellsPost-Golgi traffickingCell surfacePolarized epithelial cellsEpithelial cellsMDCK epithelial cellsDistinct trafficking routesBiosynthetic traffickingCarrier vesiclesSecretory pathwayMembrane proteinsSurface deliveryBasolateral domainMost proteinsTrafficking routesGolgi complexTemperature blockTraffickingProteinMembraneCells
2011
Polycystin-2 and phosphodiesterase 4C are components of a ciliary A-kinase anchoring protein complex that is disrupted in cystic kidney diseases
Choi YH, Suzuki A, Hajarnis S, Ma Z, Chapin HC, Caplan MJ, Pontoglio M, Somlo S, Igarashi P. Polycystin-2 and phosphodiesterase 4C are components of a ciliary A-kinase anchoring protein complex that is disrupted in cystic kidney diseases. Proceedings Of The National Academy Of Sciences Of The United States Of America 2011, 108: 10679-10684. PMID: 21670265, PMCID: PMC3127890, DOI: 10.1073/pnas.1016214108.Peer-Reviewed Original ResearchConceptsPolycystin-2Primary ciliaA-kinase anchoring protein 150Dysregulation of cAMPTranscription factor hepatocyte nuclear factor-1βCystic kidney diseasePolycystic kidney diseaseCAMP levelsAKAP complexesRenal primary ciliaRenal epithelial cellsProtein complexesSensory organellesHuman polycystic kidney diseaseC-terminusProtein 150Hepatocyte nuclear factor-1βCalcium channel activityCell surfaceChannel activityCiliaKidney cystsKidney cellsDifferent gene mutationsEpithelial cells
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 ResearchConceptsK-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 expressionProteinReticulumVisualizing Protein Trafficking: Membrane Proteins Follow Multiple Trafficking Pathways to the Basolateral Cell Surface in Polarized Epithelial Cells
Farr G, Alves D, Stoops E, Hull M, Caplan M. Visualizing Protein Trafficking: Membrane Proteins Follow Multiple Trafficking Pathways to the Basolateral Cell Surface in Polarized Epithelial Cells. Microscopy And Microanalysis 2010, 16: 958-959. DOI: 10.1017/s1431927610053560.Peer-Reviewed Original ResearchPolarized traffic towards the cell surface: how to find the route
Carmosino M, Valenti G, Caplan M, Svelto M. Polarized traffic towards the cell surface: how to find the route. Biology Of The Cell 2010, 102: 75-91. PMID: 19909237, DOI: 10.1042/bc20090134.Peer-Reviewed Original Research
2009
Chapter 11 Detecting the Surface Localization and Cytoplasmic Cleavage of Membrane-Bound Proteins
Chapin HC, Rajendran V, Capasso A, Caplan MJ. Chapter 11 Detecting the Surface Localization and Cytoplasmic Cleavage of Membrane-Bound Proteins. Methods In Cell Biology 2009, 94: 223-239. PMID: 20362093, PMCID: PMC3063071, DOI: 10.1016/s0091-679x(08)94011-5.Peer-Reviewed Original ResearchConceptsC-terminal tailPolycystin-1Membrane-bound proteinsSubcellular localizationNuclear localizationPlasma membranePC1 proteinCytoplasmic cleavagePhysiological functionsSurface localizationFunctional roleSurface proteinsCell surfaceSurface populationsSpecific cleavageProteinImmunofluorescence protocolSoluble fragmentProtein expressionCell populationsImportant poolAutosomal dominant polycystic kidney diseasePolycystic kidney diseaseCleavageComplete understandingMembrane proteins follow multiple pathways to the basolateral cell surface in polarized epithelial cells
Farr GA, Hull M, Mellman I, Caplan MJ. Membrane proteins follow multiple pathways to the basolateral cell surface in polarized epithelial cells. Journal Of Cell Biology 2009, 186: 269-282. PMID: 19620635, PMCID: PMC2717640, DOI: 10.1083/jcb.200901021.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBiological TransportCadherinsCell LineCell MembraneCell PolarityDogsEndosomesEpithelial CellsExocytosisGolgi ApparatusHumansMembrane GlycoproteinsMembrane ProteinsModels, MolecularProtein Structure, SecondaryProtein TransportReceptors, TransferrinRecombinant Fusion ProteinsSodium-Potassium-Exchanging ATPaseStaining and LabelingTrans-Golgi NetworkViral Envelope ProteinsConceptsBasolateral proteinsMembrane proteinsSurface deliveryK-ATPaseVesicular stomatitis virus G proteinPolarized epithelial cellsBasolateral membrane proteinsEpithelial cellsVirus G proteinBasolateral cell surfaceBasolateral deliveryTransport intermediatesGolgi networkSmall GTPasesPlasma membraneG proteinsCell surfaceProteinMultiple pathwaysBasolateral membraneGolgiPathwayCellsMembraneGTPases
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 2EndosomesTRANSPORT PROTEIN TRAFFICKING IN POLARIZED CELLS
Muth TR, Caplan MJ. TRANSPORT PROTEIN TRAFFICKING IN POLARIZED CELLS. Annual Review Of Cell And Developmental Biology 2003, 19: 333-366. PMID: 14570573, DOI: 10.1146/annurev.cellbio.19.110701.161425.Peer-Reviewed Original ResearchConceptsTransport proteinsMembrane trafficking processesIon transport proteinsIon transport activityProtein traffickingCellular machineryTrafficking processesPolarized cellsPlasma membraneEndocytic retrievalSubcellular distributionPhysiological functionsTransport activityCell surfaceBiochemical natureCell membraneIntracellular populationProteinMembraneTraffickingMachineryRegulationCellsDomainPolycystin-1 Distribution Is Modulated by Polycystin-2 Expression in Mammalian Cells*
Grimm DH, Cai Y, Chauvet V, Rajendran V, Zeltner R, Geng L, Avner ED, Sweeney W, Somlo S, Caplan MJ. Polycystin-1 Distribution Is Modulated by Polycystin-2 Expression in Mammalian Cells*. Journal Of Biological Chemistry 2003, 278: 36786-36793. PMID: 12840011, DOI: 10.1074/jbc.m306536200.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBlotting, WesternCell LineCell MembraneCells, CulturedCOS CellsDNA, ComplementaryEndoplasmic ReticulumGene Expression RegulationMembrane ProteinsMiceMice, TransgenicMicroscopy, FluorescenceModels, BiologicalMutationPrecipitin TestsProtein BindingProtein BiosynthesisProteinsRecombinant Fusion ProteinsRNA, MessengerTransfectionTRPP Cation ChannelsConceptsPolycystin-1Polycystin-2Mammalian cellsLevel of expressionPolycystin-2 expressionEndoplasmic reticulumCell surfaceCOS-7 cellsNull cell lineRelative expression levelsSubcellular localizationFusion proteinGradient of expressionExpression levelsProteinCell linesPolycystinsAutosomal dominant polycystic kidney diseaseDominant polycystic kidney diseaseDivergent patternsExpressionPolycystic kidney diseaseReticulumCellsLocalization
2002
Calcium-pump inhibitors induce functional surface expression of ΔF508-CFTR protein in cystic fibrosis epithelial cells
Egan ME, Glöckner-Pagel J, Ambrose C, Cahill PA, Pappoe L, Balamuth N, Cho E, Canny S, Wagner CA, Geibel J, Caplan MJ. Calcium-pump inhibitors induce functional surface expression of ΔF508-CFTR protein in cystic fibrosis epithelial cells. Nature Medicine 2002, 8: 485-492. PMID: 11984593, DOI: 10.1038/nm0502-485.Peer-Reviewed Original ResearchConceptsEndoplasmic reticulumCalcium pump inhibitorΔF508-CFTR proteinCystic fibrosis epithelial cellsCystic fibrosis transmembrane conductance regulator (CFTR) proteinCystic fibrosis cell lineFunctional surface expressionSurface expressionChaperone activityChaperone proteinsRegulator proteinPlasma membraneCystic fibrosis defectCell surfaceProteinCell linesPotential targetOptimal activityInhibitor thapsigarginEpithelial cellsExpressionCommon mutationsInhibitorsMouse modelReticulum
1998
Sorting 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 ResearchConceptsApical 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
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
1996
Real-time detection of the surface delivery of newly synthesized membrane proteins.
Andreose JS, Fumagalli G, Sigworth FJ, Caplan MJ. Real-time detection of the surface delivery of newly synthesized membrane proteins. Proceedings Of The National Academy Of Sciences Of The United States Of America 1996, 93: 7661-7666. PMID: 8755532, PMCID: PMC38803, DOI: 10.1073/pnas.93.15.7661.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBungarotoxinsCell LineCell MembraneElectrophysiologyFourier AnalysisGolgi ApparatusGuanosine 5'-O-(3-Thiotriphosphate)Guanosine TriphosphateIon ChannelsKineticsMembrane PotentialsMembrane ProteinsMiceMuscle, SkeletalProtein Processing, Post-TranslationalReceptors, NicotinicTime FactorsConceptsMembrane proteinsPlasma membraneCell surfaceDegrees C temperature blockCultured muscle cellsConstitutive trafficTransport vesiclesConstitutive deliveryFusion eventsSurface deliveryFusion poreExocytotic vesiclesAChR moleculeGolgi complexTemperature blockAChR proteinNicotinic acetylcholine receptorsIon channel propertiesMost cellsVesiclesProteinCurrent fluctuationsMuscle cellsAcetylcholine receptorsGuanosine 5'
1994
The axonal gamma-aminobutyric acid transporter GAT-1 is sorted to the apical membranes of polarized epithelial cells.
Pietrini G, Suh YJ, Edelmann L, Rudnick G, Caplan MJ. The axonal gamma-aminobutyric acid transporter GAT-1 is sorted to the apical membranes of polarized epithelial cells. Journal Of Biological Chemistry 1994, 269: 4668-4674. PMID: 8308038, DOI: 10.1016/s0021-9258(17)41828-x.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAxonsBetaineCarrier ProteinsCell CompartmentationCell LineCell MembraneCell PolarityCells, CulturedDogsEpitheliumFluorescent Antibody TechniqueGABA Plasma Membrane Transport ProteinsGamma-Aminobutyric AcidIn Vitro TechniquesMembrane ProteinsMembrane Transport ProteinsNerve Tissue ProteinsOrganic Anion TransportersConceptsGamma-aminobutyric acid (GABA) transporter GAT-1MDCK cellsDistinct cell surface domainsEpithelial Madin-Darby canine kidney (MDCK) cell lineTransporter GAT-1Cell surfaceCell surface domainsCell surface biotinylationApical cell surfaceBasolateral cell surfaceEpithelial cellsBGT-1Axonal plasma membraneCell surface membraneSorting signalsCanine kidney cell lineMadin-Darby canine kidney (MDCK) cell lineGAT-1GABA transporterDistinct subdomainsKidney cell lineBetaine transporterHyperosmotic stressSurface biotinylationApical localization
1993
Sorting of ion transport proteins in polarized cells
Gottardi C, Pietrini G, Roush D, Caplan M. Sorting of ion transport proteins in polarized cells. Journal Of Cell Science. Supplement 1993, 1993: 13-20. PMID: 8144688, DOI: 10.1242/jcs.1993.supplement_17.3.Peer-Reviewed Original ResearchConceptsIon transport proteinsTransport proteinsSorting signalsSubunit polypeptidesMultiple sorting signalsEpithelial cellsCell typesPlasma membrane domainsPolarized epithelial cellsClass of proteinsEpithelial sortingNon-epithelial cell typesCellular machineryMembrane domainsFunctional homologyPlasmalemmal domainsPlasma membraneRelated membersCell surfaceIon pumpsDistinct populationsProteinRelated familiesDelivery pathwayDistinct routesMolecular requirements for the cell-surface expression of multisubunit ion-transporting ATPases. Identification of protein domains that participate in Na,K-ATPase and H,K-ATPase subunit assembly
Gottardi CJ, Caplan MJ. Molecular requirements for the cell-surface expression of multisubunit ion-transporting ATPases. Identification of protein domains that participate in Na,K-ATPase and H,K-ATPase subunit assembly. Journal Of Biological Chemistry 1993, 268: 14342-14347. PMID: 8390991, DOI: 10.1016/s0021-9258(19)85246-8.Peer-Reviewed Original ResearchConceptsK-ATPase alpha subunitK-ATPase beta subunitAlpha subunitBeta subunitCell surface expressionTerminal halfK-ATPaseCell surface deliveryEfficient cell surface expressionK-ATPase alphaNH2-terminal halfCOS-1 cellsIon-transporting ATPasesProtein domainsK-ATPase enzymeSubunit assemblySurface deliveryIntracellular vesiclesSubunit chimerasIndividual subunitsActive enzymeMolecular requirementsSubunitsCell surfaceBeta protein
1991
Chapter 2 Biogenesis and Sorting of Plasma Membrane Proteins
Caplan M. Chapter 2 Biogenesis and Sorting of Plasma Membrane Proteins. Current Topics In Membranes 1991, 39: 37-86. PMCID: PMC7128438, DOI: 10.1016/s0070-2161(08)60800-x.Peer-Reviewed Original ResearchPlasma membrane proteinsPlasma membraneMembrane proteinsCell typesCell surfacePolarized epithelial cellsApical plasma membraneDistribution of polypeptidesExpression of genesCell surface membraneTransducer proteinsAnchor cellCell biologyProtein compositionProteinMost cellsBiogenesisFascinating questionsPlasmalemmal receptorsOrganellesEpithelial cellsSurface membranePolypeptideMembranePlasmalemma
1989
Polarized distribution of Na+,K+-ATPase in giant cells elicited in vivo and in vitro.
Vignery A, Niven-Fairchild T, Ingbar DH, Caplan M. Polarized distribution of Na+,K+-ATPase in giant cells elicited in vivo and in vitro. Journal Of Histochemistry & Cytochemistry 1989, 37: 1265-1271. PMID: 2546991, DOI: 10.1177/37.8.2546991.Peer-Reviewed Original ResearchConceptsPlasma membranePolarized distributionAdherent plasma membraneGiant cell differentiationLysosomal membrane antigenAlpha subunit synthesisSuitable model systemSpecialized functionsCell differentiationBiochemical studiesCell surfaceLysosomal componentsCell formationATPase expressionGiant cell formationModel systemATPaseExpressionCells
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 regions