2018
Newly synthesized polycystin‐1 takes different trafficking pathways to the apical and ciliary membranes
Gilder AL, Chapin HC, Padovano V, Hueschen CL, Rajendran V, Caplan MJ. Newly synthesized polycystin‐1 takes different trafficking pathways to the apical and ciliary membranes. Traffic 2018, 19: 933-945. PMID: 30125442, PMCID: PMC6237641, DOI: 10.1111/tra.12612.Peer-Reviewed Original ResearchConceptsPolycystin-1Ciliary deliveryBrefeldin AApical deliveryRenal epithelial cellsN-terminal fragmentPolycystin-2LLC-PK1 renal epithelial cellsDifferent trafficking pathwaysTrans-Golgi networkApical membraneEpithelial cellsCultured epithelial cellsTrafficking pathwaysTransmembrane proteinGolgi compartmentPrimary ciliaC-terminal fragmentCiliary membraneC-terminusAutocatalytic cleavageDistinct pathwaysIncubating cellsCell membraneAutosomal dominant polycystic kidney disease
2016
Newly synthesized and recycling pools of the apical protein gp135 do not occupy the same compartments
Stoops EH, Hull M, Caplan MJ. Newly synthesized and recycling pools of the apical protein gp135 do not occupy the same compartments. Traffic 2016, 17: 1272-1285. PMID: 27649479, PMCID: PMC5123909, DOI: 10.1111/tra.12449.Peer-Reviewed Original ResearchConceptsApical early endosomesPlasma membrane proteinsPolarized epithelial cellsApical recycling endosomesDistinct trafficking pathwaysSNAP-tag systemBasolateral membrane domainsProtein sortingApical proteinsRecycling endosomesTrafficking pathwaysGolgi networkProtein trafficMembrane domainsMembrane proteinsEarly endosomesPlasma membraneInitial traffickingEndosomesApical membraneProteinGp135Same compartmentEpithelial cellsTrafficking
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 spotsCellsTrafficking
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 medullaColocalize
2008
Exon Loss Accounts for Differential Sorting of Na-K-Cl Cotransporters in Polarized Epithelial Cells
Carmosino M, Giménez I, Caplan M, Forbush B. Exon Loss Accounts for Differential Sorting of Na-K-Cl Cotransporters in Polarized Epithelial Cells. Molecular Biology Of The Cell 2008, 19: 4341-4351. PMID: 18667527, PMCID: PMC2555935, DOI: 10.1091/mbc.e08-05-0478.Peer-Reviewed Original ResearchConceptsDileucine motifNa-K-Cl cotransporterRenal Na-K-Cl cotransporterPolarized epithelial cellsAmino acid stretchApical proteinsApical sortingEvolutionary lossRenal epithelial cell lineGene structurePhylogenetic analysisDifferential sortingDirect traffickingEpithelial cell lineAdditional exonC-terminusMammalian kidneyApical membraneExonsNovel mechanismNKCC2 geneCell linesBasolateral membraneMotifEpithelial cellsApical membrane expression of NKCC2 is directed by a domain within its cytoplasmic C‐terminus
Carmosino M, Gimenez I, Caplan M, Forbush B. Apical membrane expression of NKCC2 is directed by a domain within its cytoplasmic C‐terminus. The FASEB Journal 2008, 22: 935.4-935.4. DOI: 10.1096/fasebj.22.1_supplement.935.4.Peer-Reviewed Original ResearchC-terminusNa-K-Cl cotransporterMolecular basisRenal Na-K-Cl cotransporterMDCK cellsCytoplasmic C-terminusTransient expression analysisApical membrane expressionRenal epithelial cell lineBasolateral traffickingResidue stretchEpithelial cell lineApical localizationExpression analysisCentral playerMammalian kidneyApical expressionApical membraneMembrane expressionCorresponding regionLimb cellsCell linesBasolateral membraneThick ascending limb cellsNKCC2
2006
An Extracellular Loop of the Human Non-Gastric H,K-ATPase a-subunit is Involved in Apical Plasma Membrane Polarization
Lerner M, Lemke D, Bertram H, Schillers H, Oberleithner H, Caplan MJ, Reinhardt J. An Extracellular Loop of the Human Non-Gastric H,K-ATPase a-subunit is Involved in Apical Plasma Membrane Polarization. Cellular Physiology And Biochemistry 2006, 18: 75-84. PMID: 16914892, DOI: 10.1159/000095169.Peer-Reviewed Original ResearchConceptsP-type ATPasesSorting motifApical deliveryExtracellular loopK-ATPaseSpecific sorting signalsPlasma membrane polarizationShort extracellular loopApical plasma membraneMadin-Darby canine kidney cellsSingle point mutationCanine kidney cellsSorting signalsGene familyPlasma membraneFlanking regionsEpithelial apical membraneK-ATPasesPhysiological roleApical membraneCellular distributionPoint mutationsIon pumpsATP1AL1Corresponding regionCFTR is required for PKA-regulated ATP sensitivity of Kir1.1 potassium channels in mouse kidney
Lu M, Leng Q, Egan ME, Caplan MJ, Boulpaep EL, Giebisch GH, Hebert SC. CFTR is required for PKA-regulated ATP sensitivity of Kir1.1 potassium channels in mouse kidney. Journal Of Clinical Investigation 2006, 116: 797-807. PMID: 16470247, PMCID: PMC1361349, DOI: 10.1172/jci26961.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAnimalsCurcuminCyclic AMP-Dependent Protein KinasesCystic Fibrosis Transmembrane Conductance RegulatorHydrogen-Ion ConcentrationKidneyMiceMice, Inbred C57BLMice, Inbred CFTRMice, TransgenicMutationOocytesPatch-Clamp TechniquesPotassium Channels, Inwardly RectifyingXenopus laevisConceptsFunctional switchCystic fibrosis transmembrane conductance regulator (CFTR) Cl(-) channelATP sensitivityEffects of CFTRThick ascending limbPotential physiological rolePKA activityRenal K channelsCystic fibrosisPhysiological roleSecretory channelsK channelsRenal tubule epithelial cellsApical membraneCFTRDeltaF508 mutationDistal nephron segmentsCl- channelsK homeostasisTubule epithelial cellsEpithelial cellsTAL cellsPotassium channelsK handlingGlibenclamide sensitivity
2004
Sorting of H,K‐ATPase β‐Subunit in MDCK and LLC‐PK1 Cells is Independent of μ1B Adaptin Expression
Duffield A, Fölsch H, Mellman I, Caplan MJ. Sorting of H,K‐ATPase β‐Subunit in MDCK and LLC‐PK1 Cells is Independent of μ1B Adaptin Expression. Traffic 2004, 5: 449-461. PMID: 15117319, DOI: 10.1111/j.1398-9219.2004.00192.x.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Protein Complex mu SubunitsAdaptor Proteins, Vesicular TransportAmino Acid MotifsAnimalsCell LineCytoplasmDogsEpithelial CellsGlutathione TransferaseH(+)-K(+)-Exchanging ATPaseLLC-PK1 CellsMembrane ProteinsProtein SubunitsProtein TransportReceptors, LDLReceptors, TransferrinRecombinant Fusion ProteinsSwineTransfectionTyrosineConceptsLow-density lipoproteinTransferrin receptorBasolateral localizationTyrosine-based motifMDCK cellsB expressionLLC-PK1 cellsEpithelial cellsLipoproteinMadin-Darby canine kidney cellsCertain epithelial cellsReceptorsKidney cellsCanine kidney cellsK-ATPase beta subunitCellsDifferential expressionK-ATPaseBasolateral expressionExpressionApical membrane
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 mutationMembrane
1998
Tyrosine-based Membrane Protein Sorting Signals Are Differentially Interpreted by Polarized Madin-Darby Canine Kidney and LLC-PK1 Epithelial Cells*
Roush D, Gottardi C, Naim H, Roth M, Caplan M. Tyrosine-based Membrane Protein Sorting Signals Are Differentially Interpreted by Polarized Madin-Darby Canine Kidney and LLC-PK1 Epithelial Cells*. Journal Of Biological Chemistry 1998, 273: 26862-26869. PMID: 9756932, DOI: 10.1074/jbc.273.41.26862.Peer-Reviewed Original ResearchConceptsProtein sorting signalsTyrosine-based motifLLC-PK1 cellsCytoplasmic tailSorting signalsMDCK cellsApical membraneBeta-subunit polypeptidesBasolateral membraneK-ATPase beta subunitDi-leucine motifBeta subunit proteinLLC-PK1 epithelial cellsMadin-Darby canine kidney cellsMadin-Darby canine kidneyEpithelial cell typesCanine kidney cellsK-ATPase betaHA-Y543Cytoplasmic sequencesSequence motifsSubunit polypeptidesMembrane proteinsBasolateral domainPolarized epithelium
1996
Immunolocalization of ion transport proteins in human autosomal dominant polycystic kidney epithelial cells.
Brill SR, Ross KE, Davidow CJ, Ye M, Grantham JJ, Caplan MJ. Immunolocalization of ion transport proteins in human autosomal dominant polycystic kidney epithelial cells. Proceedings Of The National Academy Of Sciences Of The United States Of America 1996, 93: 10206-10211. PMID: 8816777, PMCID: PMC38362, DOI: 10.1073/pnas.93.19.10206.Peer-Reviewed Original ResearchConceptsCyst epithelial cellsEpithelial cellsCystic fibrosis transmembrane conductance regulatorIon transport proteinsFibrosis transmembrane conductance regulatorK-ATPaseApical cystic fibrosis transmembrane conductance regulatorTransmembrane conductance regulatorKidney epithelial cellsK-ATPase proteinRenal epithelial cellsCFTR proteinTransport proteinsConductance regulatorIntracellular structuresFluid-filled cystsApical membraneForskolin treatmentBasolateral surfacePermeable filter supportsApical surfaceProteinCl- channelsApical labelingAutosomal dominant polycystic kidney diseasePolarized Expression of GABA Transporters in Madin-Darby Canine Kidney Cells and Cultured Hippocampal Neurons (∗)
Ahn J, Mundigl O, Muth T, Rudnick G, Caplan M. Polarized Expression of GABA Transporters in Madin-Darby Canine Kidney Cells and Cultured Hippocampal Neurons (∗). Journal Of Biological Chemistry 1996, 271: 6917-6924. PMID: 8636119, DOI: 10.1074/jbc.271.12.6917.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsAxonsBase SequenceCarrier ProteinsCell LineDNA PrimersDNA, ComplementaryDogsGABA Plasma Membrane Transport ProteinsGamma-Aminobutyric AcidHippocampusKidneyMembrane ProteinsMembrane Transport ProteinsMicroinjectionsMolecular Sequence DataNeuronsOrganic Anion TransportersConceptsMadin-Darby canine kidney cellsCanine kidney cellsMDCK cellsBetaine transporterMembrane protein sortingAmino acid sequence identityApical membraneCell surface biotinylationGAT-2GABA transporterKidney cellsGamma-aminobutyric acid transporterEpithelial cellsProtein sortingGAT-1Polarized neuronsSurface biotinylationSequence identityAcid transportersCultured hippocampal neuronsHippocampal neuronsPolarized expressionCell typesTransporter GAT-1Basolateral surface
1995
Developmental regulation of membrane protein sorting in Drosophila embryos
Shiel MJ, Caplan MJ. Developmental regulation of membrane protein sorting in Drosophila embryos. American Journal Of Physiology 1995, 269: c207-c216. PMID: 7631747, DOI: 10.1152/ajpcell.1995.269.1.c207.Peer-Reviewed Original ResearchConceptsDrosophila embryosMembrane proteinsSurface ectodermTransgenic Drosophila embryosVesicular stomatitis virus G proteinDrosophila melanogaster embryosMammalian epithelial cellsPlacental alkaline phosphataseApical plasma membraneVirus G proteinBasolateral proteinsSorting pathwaysCytosolic portionDevelopmental regulationHuman placental alkaline phosphatasePlasma membraneBasolateral distributionChimeric constructsSubcellular distributionG proteinsApical membraneInternal epitheliumEmbryosProteinApical surface