2015
The periciliary ring in polarized epithelial cells is a hot spot for delivery of the apical protein gp135
Stoops EH, Hull M, Olesen C, Mistry K, Harder JL, Rivera-Molina F, Toomre D, Caplan MJ. The periciliary ring in polarized epithelial cells is a hot spot for delivery of the apical protein gp135. Journal Of Cell Biology 2015, 211: 287-294. PMID: 26504168, PMCID: PMC4621837, DOI: 10.1083/jcb.201502045.Peer-Reviewed Original ResearchConceptsPrimary ciliaSurface proteinsTrans-Golgi networkPolarized epithelial cellsApical surface proteinsSNAP-tag systemBasolateral plasma membraneCell surface proteinsEpithelial cellsApical proteinsPericiliary regionGolgi networkPolarized traffickingCarrier vesiclesProtein deliveryPlasma membraneApical membraneProteinGp135Basolateral membraneCiliaMembraneHot spotsCellsTraffickingDual 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
2014
SNAP-Tag to Monitor Trafficking of Membrane Proteins in Polarized Epithelial Cells
Stoops EH, Farr GA, Hull M, Caplan MJ. SNAP-Tag to Monitor Trafficking of Membrane Proteins in Polarized Epithelial Cells. Methods In Molecular Biology 2014, 1174: 171-182. PMID: 24947381, DOI: 10.1007/978-1-4939-0944-5_11.Peer-Reviewed Original ResearchConceptsMembrane proteinsSNAP-tagTrans-Golgi networkPolarized epithelial cellsBasolateral membrane proteinsSNAP-tag systemEpithelial cellsFluorescence microscopic analysisBiochemical approachesPlasma membraneTrafficking routesSubcellular distributionProteinConfocal microscopySDS-PAGEMicroscopic analysisTagsCellsTraffickingTag systemMembranePool
2013
Chapter 1 Epithelial Cell Structure and Polarity
Matlin K, Caplan M. Chapter 1 Epithelial Cell Structure and Polarity. 2013, 3-43. DOI: 10.1016/b978-0-12-381462-3.00001-x.Peer-Reviewed Original Research
2012
AS160: a new Na,K‐ATPase partner that regulates the trafficking of the sodium pump in response to energy depletion and renal ischemia
Alves D, Thulin G, Loffing J, Kashgarian M, Caplan M. AS160: a new Na,K‐ATPase partner that regulates the trafficking of the sodium pump in response to energy depletion and renal ischemia. The FASEB Journal 2012, 26: lb808-lb808. DOI: 10.1096/fasebj.26.1_supplement.lb808.Peer-Reviewed Original ResearchPlasma membraneRenal epithelial cellsK-ATPaseEpithelial cellsCytoplasmic vesicular compartmentsDifferent cellular poolsCultured epithelial cellsVesicular compartmentsWild typeCellular poolAS160Cytoplasmic accumulationKnockout micePhysiological roleWild-type controlsEnergy depletionRenal ischemiaPhysiological stimuliType controlsCellular NaK-ATPase activityIntracellular accumulationMembraneIschemic kidney injuryCells
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 Ca2MembraneAfadinExtracellularInhibitionRegulated Intramembrane Proteolysis: Signaling Pathways and Biological Functions
Lal M, Caplan M. Regulated Intramembrane Proteolysis: Signaling Pathways and Biological Functions. Physiology 2011, 26: 34-44. PMID: 21357901, DOI: 10.1152/physiol.00028.2010.Peer-Reviewed Original ResearchConceptsFundamental cellular processesIntegral membrane proteinsFunctional protein domainsCellular processesProtein domainsElicit biological responsesMembrane proteinsTransmembrane proteinIntramembrane cleavageBiological functionsPhysiological processesProteolytic cleavageBiological responsesProteinCleavageDomainMessengerEnzymePathwayMembrane
2010
MAL/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 medullaColocalizePolarized 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
Membrane 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
TRANSPORT 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 populationProteinMembraneTraffickingMachineryRegulationCellsDomain
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
2001
The NH2-terminus of Norepinephrine Transporter Contains a Basolateral Localization Signal for Epithelial Cells
Gu H, Wu X, Giros B, Caron M, Caplan M, Rudnick G. The NH2-terminus of Norepinephrine Transporter Contains a Basolateral Localization Signal for Epithelial Cells. Molecular Biology Of The Cell 2001, 12: 3797-3807. PMID: 11739781, PMCID: PMC60756, DOI: 10.1091/mbc.12.12.3797.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsCell LineCell PolarityDogsDopamine Plasma Membrane Transport ProteinsEpithelial CellsHumansMembrane GlycoproteinsMembrane Transport ProteinsMiceMicroscopy, ConfocalMolecular Sequence DataMutagenesis, Site-DirectedNerve Tissue ProteinsNorepinephrine Plasma Membrane Transport ProteinsProtein Sorting SignalsSequence AlignmentSymportersConceptsBasolateral localization signalLocalization signalDileucine motifPlasma membraneBasolateral localizationOverall amino acid sequence identityAmino acid sequence identityTerminal regionMDCK cellsApical plasma membraneBasolateral membraneEpithelial cellsSequence identityApical localizationChimeric proteinTransport assaysTransporter localizationAmino acidsApical membraneNorepinephrine transporterTransportersCorresponding sequenceDopamine transporterSame mutationMembraneIon pump sorting in polarized renal epithelial cells
Caplan M. Ion pump sorting in polarized renal epithelial cells. Kidney International 2001, 60: 427-430. PMID: 11473621, DOI: 10.1046/j.1523-1755.2001.060002427.x.Peer-Reviewed Original ResearchConceptsIon transport proteinsRenal epithelial cellsSubcellular localizationTransport proteinsPolarized renal epithelial cellsEpithelial cellsProtein subcellular localizationBasolateral domainMultiple complex signalsPlasma membranePolarized distributionIon pumpsProteinCellsMembraneLocalizationDomain
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
Ion pumps in epithelial cells: sorting, stabilization, and polarity
Caplan MJ. Ion pumps in epithelial cells: sorting, stabilization, and polarity. American Journal Of Physiology 1997, 272: g1304-g1313. PMID: 9227464, DOI: 10.1152/ajpgi.1997.272.6.g1304.Peer-Reviewed Original ResearchMembrane polarity in epithelial cells: protein sorting and establishment of polarized domains
Caplan MJ. Membrane polarity in epithelial cells: protein sorting and establishment of polarized domains. American Journal Of Physiology 1997, 272: f425-f429. PMID: 9140041, DOI: 10.1152/ajprenal.1997.272.4.f425.Peer-Reviewed Original ResearchConceptsTransport proteinsEpithelial cellsDistinct surface domainsEpithelial cell typesProtein sortingBiological specializationCellular pathwaysPlasma membranePolarized epitheliumElegant networkMembrane polarityCell typesBasolateral surfaceDistinct populationsProteinBasolateral portionPhysiological propertiesSurface domainsCellsAbsolute prerequisiteDomainPlasmalemmaPathwaySortingMembrane
1995
The generation of epithelial polarity in mammalian and Drosophila embryos
Shiel M, Caplan M. The generation of epithelial polarity in mammalian and Drosophila embryos. Seminars In Cell And Developmental Biology 1995, 6: 39-46. DOI: 10.1016/s1044-5781(06)80083-6.Peer-Reviewed Original Research
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
1991
Distinct pathways for basolateral targeting of membrane and secretory proteins in polarized epithelial cells.
Boll W, Partin JS, Katz AI, Caplan MJ, Jamieson JD. Distinct pathways for basolateral targeting of membrane and secretory proteins in polarized epithelial cells. Proceedings Of The National Academy Of Sciences Of The United States Of America 1991, 88: 8592-8596. PMID: 1656451, PMCID: PMC52555, DOI: 10.1073/pnas.88.19.8592.Peer-Reviewed Original ResearchConceptsCarrier vesiclesMembrane proteinsBasolateral domainSecretory proteinsMadin-Darby canine kidney II cell linePolarized epithelial cellsBasement membrane protein lamininEpithelial cellsBasolateral proteinsBasolateral targetingProtein lamininMicrotubule disruptionDistinct pathwaysMicrotubule depolymerizationProteinDistinct setsCell linesBinding sitesBasolateral secretionIntegrinsVesiclesLamininPathwayMembraneCells