2020
Mechanisms involved in AMPK-mediated deposition of tight junction components to the plasma membrane
Wu J, Rowart P, Jouret F, Gassaway BM, Rajendran V, Rinehart J, Caplan MJ. Mechanisms involved in AMPK-mediated deposition of tight junction components to the plasma membrane. American Journal Of Physiology - Cell Physiology 2020, 318: c486-c501. PMID: 31913699, PMCID: PMC7099514, DOI: 10.1152/ajpcell.00422.2019.Peer-Reviewed Original ResearchMeSH KeywordsAMP-Activated Protein KinasesAnimalsCell MembraneDogsMadin Darby Canine Kidney CellsMicePhosphorylationProtein Kinase CTight JunctionsZonula Occludens-1 ProteinConceptsJunction assemblyPlasma membranePhospho-defective mutantsEpithelial junction assemblyMDCK renal epithelial cellsProtein kinase activationJunction-associated proteinsRenal epithelial cellsActive GTPEpithelial polarizationTight junction componentsZO-1 localizationAMPK activationKinase activationKey regulatorAfadinAMPKImportant regulatorJunction componentsProtein zonula occludens-1Par3Epithelial cellsTight junction protein zonula occludens-1RegulatorAssembly
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 ResearchMeSH KeywordsAnimalsCell MembraneCell PolarityContactin 1DogsEndosomesGolgi ApparatusHumansMadin Darby Canine Kidney CellsProtein TransportConceptsApical 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 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 blockTraffickingProteinMembraneCellsAkt Substrate of 160 kD Regulates Na+,K+-ATPase Trafficking in Response to Energy Depletion and Renal Ischemia
Alves DS, Thulin G, Loffing J, Kashgarian M, Caplan MJ. Akt Substrate of 160 kD Regulates Na+,K+-ATPase Trafficking in Response to Energy Depletion and Renal Ischemia. Journal Of The American Society Of Nephrology 2015, 26: 2765-2776. PMID: 25788531, PMCID: PMC4625659, DOI: 10.1681/asn.2013101040.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBiotinylationCell LineCytoplasmDogsDynaminsEndocytosisEpithelial CellsGTPase-Activating ProteinsHumansIschemiaKidneyKidney DiseasesMadin Darby Canine Kidney CellsMaleMiceMice, KnockoutMicroscopy, FluorescencePhosphorylationProtein TransportReperfusion InjuryRNA, Small InterferingSignal TransductionSodium-Potassium-Exchanging ATPaseConceptsRenal epithelial cellsATPase traffickingIntracellular compartmentsEpithelial cell polarityEpithelial cellsBasolateral plasma membraneGlucose transporter 4Cultured epithelial cellsCell polarityRab GTPaseAkt substratePlasma membraneSubcellular distributionAS160Energy depletionDirect bindingTransporter 4TraffickingDirect roleK-ATPaseATPaseTubular soluteIntracellular accumulationCellsCompartments
2013
Epithelial morphogenesis of MDCK cells in three-dimensional collagen culture is modulated by interleukin-8
Wells EK, Yarborough O, Lifton RP, Cantley LG, Caplan MJ. Epithelial morphogenesis of MDCK cells in three-dimensional collagen culture is modulated by interleukin-8. American Journal Of Physiology - Cell Physiology 2013, 304: c966-c975. PMID: 23485708, PMCID: PMC3651639, DOI: 10.1152/ajpcell.00261.2012.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCell Culture TechniquesCell LineDogsEpithelial CellsGene ExpressionHepatocyte Growth FactorInterleukin-8KidneyMadin Darby Canine Kidney CellsMorphogenesisRNA, MessengerUp-RegulationConceptsMDCK cellsEpithelial morphogenesisHepatocyte growth factorGene expressionMDCK culturesDifferential gene expressionThree-dimensional collagen culturesReal-time PCR analysisGreater expression differencesMDCK cystsRenal epithelial cellsCollagen gelsGene setsTwo-dimensional cultureExpression differencesHGF stimulationThree-dimensional cultureMicroarray analysisSpherical cystsIL-8 protein expressionPCR analysisTubule-like structuresIL-8 participatesCollagen culturesProtein levels
2012
VIP17/MAL expression modulates epithelial cyst formation and ciliogenesis
Takiar V, Mistry K, Carmosino M, Schaeren-Wiemers N, Caplan MJ. VIP17/MAL expression modulates epithelial cyst formation and ciliogenesis. American Journal Of Physiology - Cell Physiology 2012, 303: c862-c871. PMID: 22895261, PMCID: PMC3469709, DOI: 10.1152/ajpcell.00338.2011.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCiliaDogsEpithelial CellsMadin Darby Canine Kidney CellsMiceMice, TransgenicMyelin and Lymphocyte-Associated Proteolipid ProteinsPolycystic Kidney DiseasesConceptsRenal cystogenesisPrimary ciliaVectorial solute transportApical vesicle transportConsequence of defectsEpithelial cellsEpithelial cyst formationPolarized organizationRenal epithelial cellsBasolateral markersVesicle transportIntegral proteinsAbsent ciliaCiliary defectsExpression resultsAberrant sortingCiliary morphologyOverexpressing cellsImmunofluorescence analysisCiliaCystogenesisCiliogenesisOverexpressionCyst developmentTransgenic mice