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
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
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
2011
Regulated 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
Polycystin-1 Surface Localization Is Stimulated by Polycystin-2 and Cleavage at the G Protein-coupled Receptor Proteolytic Site
Chapin HC, Rajendran V, Caplan MJ. Polycystin-1 Surface Localization Is Stimulated by Polycystin-2 and Cleavage at the G Protein-coupled Receptor Proteolytic Site. Molecular Biology Of The Cell 2010, 21: 4338-4348. PMID: 20980620, PMCID: PMC3002387, DOI: 10.1091/mbc.e10-05-0407.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBlotting, WesternCell MembraneCiliaFluorescent Antibody TechniqueHEK293 CellsHumansImmunoprecipitationKidneyLLC-PK1 CellsMutationPolycystic Kidney, Autosomal DominantProtein BindingProtein IsoformsProtein Processing, Post-TranslationalProtein Structure, TertiaryProtein TransportSwineTRPP Cation ChannelsConceptsG-protein-coupled receptor proteolytic siteGPS cleavagePC2 channel activitySurface deliveryChannel activityProteolytic siteSurface localizationPlasma membrane localizationC-terminal tailHuman embryonic kidney 293 cellsEmbryonic kidney 293 cellsPC2 mutationsKidney 293 cellsMembrane localizationSecretory pathwayMembrane proteinsBinding partnerTerminal tailPolycystin-2Effect of PC2Plasma membraneCiliary membraneTRP familyLLC-PK cellsCation channelsExosome 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 metastasisCD9WntVisualizing 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 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
2008
Epithelial junctions and polarity: complexes and kinases
Caplan MJ, Seo-Mayer P, Zhang L. Epithelial junctions and polarity: complexes and kinases. Current Opinion In Nephrology & Hypertension 2008, 17: 506-512. PMID: 18695392, PMCID: PMC3057677, DOI: 10.1097/mnh.0b013e32830baaae.Peer-Reviewed Original ResearchConceptsEpithelial cell polarityCell polarityEpithelial cell polarizationJunctional complexesIntercellular adhesion junctionsImportant physiological ramificationsCalcium-dependent adhesion proteinCell-cell contactCellular energy metabolismProtein complexesMembrane proteinsAdhesion junctionsPlasmalemmal domainsAdhesion proteinsCell polarizationPhysiological ramificationsEpithelial junctionsKinaseEnergy metabolismCharacteristic polarityEpithelial cellsProteinParacellular permeabilityNovel classComplexes
2007
MAL decreases the internalization of the aquaporin-2 water channel
Kamsteeg EJ, Duffield AS, Konings IB, Spencer J, Pagel P, Deen PM, Caplan MJ. MAL decreases the internalization of the aquaporin-2 water channel. Proceedings Of The National Academy Of Sciences Of The United States Of America 2007, 104: 16696-16701. PMID: 17940053, PMCID: PMC2034241, DOI: 10.1073/pnas.0708023104.Peer-Reviewed Original ResearchConceptsAquaporin-2 water channelIntracellular vesiclesApical membrane proteinsMembrane-associated proteinsTrafficking of AQP2Apical surface expressionEpithelial cellsCell surface retentionApical plasma membraneInvolvement of MALBody water homeostasisS256 phosphorylationWater channel proteinsSurface expressionApical deliveryRegulated traffickingSorting eventsRenal epithelial cellsMembrane associationMembrane proteinsPosttranslational modificationsProtein interactionsPlasma membraneChannel proteinsWater channelsTetraspan 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
2000
A Transmembrane Segment Determines the Steady-State Localization of an Ion-Transporting Adenosine Triphosphatase
Dunbar L, Aronson P, Caplan M. A Transmembrane Segment Determines the Steady-State Localization of an Ion-Transporting Adenosine Triphosphatase. Journal Of Cell Biology 2000, 148: 769-778. PMID: 10684257, PMCID: PMC2169368, DOI: 10.1083/jcb.148.4.769.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBiological TransportCationsCell LineCell MembraneCell PolarityGlycosphingolipidsGlycosylphosphatidylinositolsH(+)-K(+)-Exchanging ATPaseHydrogen-Ion ConcentrationMembrane ProteinsMolecular Sequence DataOuabainParietal Cells, GastricProtein Sorting SignalsRecombinant Fusion ProteinsSequence AlignmentSequence DeletionSodium-Potassium-Exchanging ATPaseSolubilityTransfectionConceptsK-ATPase alpha subunitAlpha subunitTransmembrane domainPolytopic membrane transport proteinK-ATPaseApical distributionGlycosphingolipid-rich membrane domainsDetergent-insoluble complexesMembrane transport proteinsApical membrane proteinsApical plasma membraneK-ATPase alphaFourth transmembrane domainLocalization signalChimeric pumpsFourth transmembraneTransmembrane segmentsK-ATPase sequencesMembrane compartmentsMembrane domainsMembrane proteinsSequence domainsPlasma membraneGastric parietal cellsTransport proteins
1998
Identification of Sorting Determinants in the C-terminal Cytoplasmic Tails of the γ-Aminobutyric Acid Transporters GAT-2 and GAT-3*
Muth T, Ahn J, Caplan M. Identification of Sorting Determinants in the C-terminal Cytoplasmic Tails of the γ-Aminobutyric Acid Transporters GAT-2 and GAT-3*. Journal Of Biological Chemistry 1998, 273: 25616-25627. PMID: 9748227, DOI: 10.1074/jbc.273.40.25616.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBiological TransportCarrier ProteinsCells, CulturedCloning, MolecularDogsFluorescent Antibody TechniqueGABA Plasma Membrane Transport ProteinsGamma-Aminobutyric AcidGenes, mycIon ChannelsKidneyMembrane ProteinsMembrane Transport ProteinsMicroscopy, ConfocalMolecular Sequence DataRecombinant Fusion ProteinsSequence DeletionConceptsC-terminal cytoplasmic tailIon transport proteinsMadin-Darby canine kidney cellsCytoplasmic tailMembrane proteinsC-terminusCanine kidney cellsTransporter familyAmino acidsBasolateral distributionTransport proteinsGAT-2Polytopic membrane proteinsProtein-based signalsProtein-protein interactionsTerminal cytoplasmic tailC-terminal sequencesKidney cellsClass of polypeptidesEpithelial cellsApical sortingPDZ domainChimeric transportersPolarized sortingSorting determinantTyrosine-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
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'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
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
1993
An ion-transporting ATPase encodes multiple apical localization signals.
Gottardi CJ, Caplan MJ. An ion-transporting ATPase encodes multiple apical localization signals. Journal Of Cell Biology 1993, 121: 283-293. PMID: 8385670, PMCID: PMC2200096, DOI: 10.1083/jcb.121.2.283.Peer-Reviewed Original ResearchConceptsK-ATPaseIon-transporting ATPaseDifferential subcellular distributionEpithelial cell typesEpithelial sortingEpithelial cellsEndocytosis signalLocalization signalEndocytic pathwayMembrane proteinsPlasmalemmal domainsApical localizationMolecular signalsSubcellular distributionBeta subunitRenal proximal tubular epithelial cellsCell typesIon pumpsApical surfaceDistinct populationsFull lengthBasolateral membraneProximal tubular epithelial cellsIndependent signalsTubular epithelial cells
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 secretionIntegrinsVesiclesLamininPathwayMembraneCellsChapter 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