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 ResearchConceptsJunction 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
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 diseaseImplications of AMPK in the Formation of Epithelial Tight Junctions
Rowart P, Wu J, Caplan MJ, Jouret F. Implications of AMPK in the Formation of Epithelial Tight Junctions. International Journal Of Molecular Sciences 2018, 19: 2040. PMID: 30011834, PMCID: PMC6073107, DOI: 10.3390/ijms19072040.Peer-Reviewed Original ResearchConceptsTJ assemblyPlasma membraneAMPK activationUbiquitous serine/threonine kinaseSerine/threonine kinaseBaso-lateral domainTight junctionsImplication of AMPKSelective paracellular permeabilityCell polarityThreonine kinaseDisruption of TJsProtein kinaseEnergy sensorTJ regulationΓ subunitMembrane componentsZO-1 distributionAssembly/AMPKEpithelial tight junctionsEssential roleZonula occludensKinaseEpithelial cells
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 E, Hull M, Olesen C, Mistry K, Harder J, Rivera-Molina F, Toomre D, Caplan M. The periciliary ring in polarized epithelial cells is a hot spot for delivery of the apical protein gp135. The Journal Of General Physiology 2015, 146: 1466oia69. DOI: 10.1085/jgp.1466oia69.Peer-Reviewed Original ResearchEpithelial cellsThe 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
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 systemMembranePoolTrafficking to the Apical and Basolateral Membranes in Polarized Epithelial Cells
Stoops EH, Caplan MJ. Trafficking to the Apical and Basolateral Membranes in Polarized Epithelial Cells. Journal Of The American Society Of Nephrology 2014, 25: 1375-1386. PMID: 24652803, PMCID: PMC4073435, DOI: 10.1681/asn.2013080883.Peer-Reviewed Original ResearchConceptsTrafficking routesCell type-specific variationsDistinct protein compositionTrans-Golgi networkPolarized epithelial cellsCellular trafficking pathwaysEpithelial cellsBasolateral membraneType-specific variationsBasolateral proteinsTrafficking pathwaysRecycling endosomesRenal epithelial cellsDifferent developmental statesCarrier vesiclesProtein distributionProtein compositionTransport functionProteinK-ATPaseCurrent understandingCellsPathwayRemarkable capacityDevelopmental state
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
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 ResearchConceptsRenal 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 miceAS160: 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
The γ-Secretase Cleavage Product of Polycystin-1 Regulates TCF and CHOP-Mediated Transcriptional Activation through a p300-Dependent Mechanism
Merrick D, Chapin H, Baggs JE, Yu Z, Somlo S, Sun Z, Hogenesch JB, Caplan MJ. The γ-Secretase Cleavage Product of Polycystin-1 Regulates TCF and CHOP-Mediated Transcriptional Activation through a p300-Dependent Mechanism. Developmental Cell 2011, 22: 197-210. PMID: 22178500, PMCID: PMC3264829, DOI: 10.1016/j.devcel.2011.10.028.Peer-Reviewed Original ResearchMeSH KeywordsAmyloid Precursor Protein SecretasesAnimalsApoptosisCell ProliferationCells, CulturedCystsEmbryo, NonmammalianHumansImmunoblottingImmunoprecipitationKidneyP300-CBP Transcription FactorsPhenotypePolycystic Kidney, Autosomal DominantTCF Transcription FactorsTranscription Factor CHOPTranscriptional ActivationTRPP Cation ChannelsWnt Signaling PathwayZebrafishConceptsCarboxy-terminal tailPolycystin-1P300-dependent mechanismTranscription factor TCFTranscriptional coactivator p300Cultured renal epithelial cellsΓ-secretase-mediated cleavageAutosomal dominant polycystic kidney diseaseRenal epithelial cellsTranscriptional activationZebrafish embryosCoactivator p300Γ-secretase activityNormal growth ratePKD1 expressionNull cellsProtein fragmentsCyst formationΓ-secretase inhibitionCHOP pathwayApoptosisEpithelial cellsCleavage productsPolycystic kidney diseaseExpressionPolycystin-2 and phosphodiesterase 4C are components of a ciliary A-kinase anchoring protein complex that is disrupted in cystic kidney diseases
Choi YH, Suzuki A, Hajarnis S, Ma Z, Chapin HC, Caplan MJ, Pontoglio M, Somlo S, Igarashi P. Polycystin-2 and phosphodiesterase 4C are components of a ciliary A-kinase anchoring protein complex that is disrupted in cystic kidney diseases. Proceedings Of The National Academy Of Sciences Of The United States Of America 2011, 108: 10679-10684. PMID: 21670265, PMCID: PMC3127890, DOI: 10.1073/pnas.1016214108.Peer-Reviewed Original ResearchConceptsPolycystin-2Primary ciliaA-kinase anchoring protein 150Dysregulation of cAMPTranscription factor hepatocyte nuclear factor-1βCystic kidney diseasePolycystic kidney diseaseCAMP levelsAKAP complexesRenal primary ciliaRenal epithelial cellsProtein complexesSensory organellesHuman polycystic kidney diseaseC-terminusProtein 150Hepatocyte nuclear factor-1βCalcium channel activityCell surfaceChannel activityCiliaKidney cystsKidney cellsDifferent gene mutationsEpithelial cellsActivating AMP-activated protein kinase (AMPK) slows renal cystogenesis
Takiar V, Nishio S, Seo-Mayer P, King JD, Li H, Zhang L, Karihaloo A, Hallows KR, Somlo S, Caplan MJ. Activating AMP-activated protein kinase (AMPK) slows renal cystogenesis. Proceedings Of The National Academy Of Sciences Of The United States Of America 2011, 108: 2462-2467. PMID: 21262823, PMCID: PMC3038735, DOI: 10.1073/pnas.1011498108.Peer-Reviewed Original ResearchConceptsCystic fibrosis transmembrane conductance regulatorRenal cystogenesisProtein kinaseAutosomal dominant polycystic kidney diseaseFibrosis transmembrane conductance regulatorTransmembrane conductance regulatorEpithelial cellsCyst epithelial cellsRenal cyst developmentCyst-lining epithelial cellsAMPK activationConductance regulatorRapamycin (mTOR) pathwayMammalian targetPharmacological activatorsChloride channelsMTOR pathwayCystogenesisCyst developmentKinaseAMPKContext of ADPKDSignificant arrestDominant polycystic kidney diseasePolycystic kidney disease
2010
Polycystic kidney disease: Pathogenesis and potential therapies
Takiar V, Caplan MJ. Polycystic kidney disease: Pathogenesis and potential therapies. Biochimica Et Biophysica Acta 2010, 1812: 1337-1343. PMID: 21146605, PMCID: PMC3139769, DOI: 10.1016/j.bbadis.2010.11.014.Peer-Reviewed Original ResearchConceptsAutosomal dominant polycystic kidney diseasePolycystic kidney diseaseKidney diseaseRenal tubular epithelial cellsDominant polycystic kidney diseaseNovel therapeutic targetTubular epithelial cellsFluid-filled cystsRenal cyst formationRenal functionTreatment of PKDPathogenetic pathwaysPotential therapyTherapeutic targetDisease pathogenesisClinical therapyCyst formationInherited conditionEpithelial cellsDiseasePathogenesisTherapyPrimary ciliaCystsParenchymaLymphocytes Accelerate Epithelial Tight Junction Assembly: Role of AMP-Activated Protein Kinase (AMPK)
Tang XX, Chen H, Yu S, Zhang L, Caplan MJ, Chan HC. Lymphocytes Accelerate Epithelial Tight Junction Assembly: Role of AMP-Activated Protein Kinase (AMPK). PLOS ONE 2010, 5: e12343. PMID: 20808811, PMCID: PMC2925955, DOI: 10.1371/journal.pone.0012343.Peer-Reviewed Original ResearchConceptsTJ assemblyActivation of AMPKProtein kinaseEpithelial cellsCalcium switch experimentsEpithelial cell polaritySuppression of AMPKTight junction assemblyRole of AMPMadin-Darby canine kidney cellsCellular ATP levelsCanine kidney cellsTight junctionsCell polarityApicolateral borderJunction assemblyModel cell lineAMPK activationProper formationAdjacent epithelial cellsTJ formationChemical inhibitorsCalu-3 human airway epithelial cellsHuman airway epithelial cellsMDCK cellsVisualizing 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