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
Exosome release of β-catenin: a novel mechanism that antagonizes Wnt signaling
Chairoungdua A, Smith DL, Pochard P, Hull M, Caplan MJ. Exosome release of β-catenin: a novel mechanism that antagonizes Wnt signaling. Journal Of Cell Biology 2010, 190: 1079-1091. PMID: 20837771, PMCID: PMC3101591, DOI: 10.1083/jcb.201002049.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAntigens, CDBeta CateninCadherinsCell LineExosomesGene Knockdown TechniquesGenes, ReporterGlycogen Synthase Kinase 3Glycogen Synthase Kinase 3 betaHumansKangai-1 ProteinLysosomesMembrane GlycoproteinsMiceModels, BiologicalProteasome Endopeptidase ComplexProtein Processing, Post-TranslationalProtein StabilityProtein TransportSignal TransductionTetraspanin 29TransfectionWnt ProteinsConceptsΒ-cateninΒ-catenin-mediated WntProtein degradation pathwaysCellular signaling pathwaysTetraspanin membrane proteinΒ-catenin protein levelsGlycogen synthase kinase-3βWnt/β-catenin signalingSynthase kinase-3βΒ-catenin signalingMembrane proteinsCytosolic proteinsSignaling pathwaysKinase-3βExosomal packagingExosome releaseSphingomyelinase inhibitorNovel mechanismE-cadherinDegradation pathwayProtein levelsCD82Tumor metastasisCD9Wnt
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
2007
Tetraspan proteins: regulators of renal structure and function
Caplan MJ, Kamsteeg EJ, Duffield A. Tetraspan proteins: regulators of renal structure and function. Current Opinion In Nephrology & Hypertension 2007, 16: 353-358. PMID: 17565278, DOI: 10.1097/mnh.0b013e328177b1fa.Peer-Reviewed Original ResearchConceptsProtein partnersRenal ion transport proteinsIon transport proteinsModulates cell adhesionImportant physiological ramificationsNormal glomerular architecturePartner proteinsTissue morphogenesisMembrane proteinsEndocytic internalizationTransport proteinsPhysiological processesRegulatory rolePhysiological ramificationsTransporter functionCell adhesionIntegrin moleculesTetraspan familyProteinEpithelial cellsTetraspansGlomerular architectureNovel classFunctional propertiesCells
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
1997
Cloned Catecholamine Transporters Expressed in Polarized Epithelial Cells: Sorting, Drug Sensitivity, and Ion-Coupling Stoichiometry
Gu H, Caplan MJ, Rudnick G. Cloned Catecholamine Transporters Expressed in Polarized Epithelial Cells: Sorting, Drug Sensitivity, and Ion-Coupling Stoichiometry. Advances In Pharmacology 1997, 42: 175-179. PMID: 9327872, DOI: 10.1016/s1054-3589(08)60721-8.Peer-Reviewed Original ResearchMeSH KeywordsAmphetamineAnimalsBiological TransportCarrier ProteinsCell LineCell PolarityCloning, MolecularDopamineDopamine Plasma Membrane Transport ProteinsEpithelial CellsGABA Plasma Membrane Transport ProteinsGamma-Aminobutyric AcidHumansKineticsMembrane GlycoproteinsMembrane ProteinsMembrane Transport ProteinsNerve Tissue ProteinsNorepinephrineNorepinephrine Plasma Membrane Transport ProteinsOrganic Anion TransportersRatsRecombinant Fusion ProteinsRecombinant ProteinsSerotoninSerotonin Plasma Membrane Transport ProteinsSubstrate SpecificitySwineSymportersTransfectionConceptsCell linesPolarized epithelial cellsHeterologous expression systemBiogenic amine transportersCanine kidney cellsSame cellular backgroundKidney cell lineLLC-PK1 cellsExpression systemBiogenic amine releaseCellular backgroundIntact cellsPig kidney cell lineSame cDNAInhibitor sensitivityAmine transportersCatecholamine transportersCoupling stoichiometryTransportersKidney cellsDrug sensitivityPharmacological propertiesEpithelial cellsMolecule of substrateAmine release
1996
Cell-specific Sorting of Biogenic Amine Transporters Expressed in Epithelial Cells*
Gu H, Ahn J, Caplan M, Blakely R, Levey A, Rudnick G. Cell-specific Sorting of Biogenic Amine Transporters Expressed in Epithelial Cells*. Journal Of Biological Chemistry 1996, 271: 18100-18106. PMID: 8663573, DOI: 10.1074/jbc.271.30.18100.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBiogenic AminesBiological TransportCarrier ProteinsCell CompartmentationCell MembraneCell PolarityCells, CulturedDogsDopamineDopamine Plasma Membrane Transport ProteinsEpithelial CellsHumansImmunohistochemistryMembrane GlycoproteinsMembrane Transport ProteinsNerve Tissue ProteinsNorepinephrineNorepinephrine Plasma Membrane Transport ProteinsRatsRecombinant ProteinsSerotoninSerotonin Plasma Membrane Transport ProteinsSymportersConceptsMadin-Darby canine kidneyMDCK cellsLLC-PK1 cellsNeurotransmitter transportersCell surface biotinylationConfocal immunofluorescence microscopyBasolateral membraneCell-specific mechanismsEpithelial cellsBiogenic amine transportersMembrane proteinsSurface biotinylationCDNA encodingHuman DA transporterAmine transportersImmunofluorescence microscopyBiotinylating reagentTransportersPermeable filter supportsApical surfaceImmunocytochemistry resultsBasolateral mediumSurface expressionApical sideDA transporter