2022
AMPK and Polycystic Kidney Disease Drug Development: An Interesting Off-Target Target
Caplan MJ. AMPK and Polycystic Kidney Disease Drug Development: An Interesting Off-Target Target. Frontiers In Medicine 2022, 9: 753418. PMID: 35174190, PMCID: PMC8841847, DOI: 10.3389/fmed.2022.753418.Peer-Reviewed Original ResearchCellular signaling pathwaysPolycystic kidney diseasePolycystic kidney disease mutationCellular energy useProtein kinaseMaster regulatorCellular metabolismSignaling pathwaysDisease mutationsGenetic diseasesTissue architectureEnzyme activityDramatic perturbationsAutosomal dominant polycystic kidney diseasePathwayDominant polycystic kidney diseaseNew therapeuticsMutationsRenal tissue architectureDrug developmentCellsKinaseAMPKGeneration pathwaysGenes
2017
The secretory pathway at 50: a golden anniversary for some momentous grains of silver
Matlin KS, Caplan MJ. The secretory pathway at 50: a golden anniversary for some momentous grains of silver. Molecular Biology Of The Cell 2017, 28: 229-232. PMID: 28082520, PMCID: PMC5231891, DOI: 10.1091/mbc.e16-07-0508.Peer-Reviewed Original ResearchConceptsSecretory pathwayBiosynthetic machineryMembrane protein trafficSpecialized cell typesCell's biosynthetic machineryModern cell biologyProtein trafficCell biologyCell typesMorphological methodologiesPathological consequencesPathwayMachineryCentral paradigmBiologyDynamic natureSecretoryCulmination of decadesCellsAdaptationDiscovery
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
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
AS160: 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
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 membraneGolgiPathwayCellsMembraneGTPasesThe uptake and intracellular fate of PLGA nanoparticles in epithelial cells
Cartiera MS, Johnson KM, Rajendran V, Caplan MJ, Saltzman WM. The uptake and intracellular fate of PLGA nanoparticles in epithelial cells. Biomaterials 2009, 30: 2790-2798. PMID: 19232712, PMCID: PMC3195413, DOI: 10.1016/j.biomaterials.2009.01.057.Peer-Reviewed Original ResearchConceptsEpithelial cellsCell linesRenal proximal tubulesType of epitheliumParticle/cell ratiosCaco-2 cellsEpithelial cell lineIntracellular fateProximal tubulesRespiratory airwaysCell ratioImmunofluorescence techniqueOK cellsDifferent epithelial cell linesEndoplasmic reticulumConfocal analysisMajor targetConfocal microscopyExtent of uptakeCellsParticle uptakeEarly endosomesCellular uptakePLGA nanoparticlesUptakeDystroglycan and AMP Kinase: Polarity's Protectors when the Power Goes Out
Zhang L, Seo-Mayer P, Caplan MJ. Dystroglycan and AMP Kinase: Polarity's Protectors when the Power Goes Out. Developmental Cell 2009, 16: 1-2. PMID: 19154710, PMCID: PMC2997531, DOI: 10.1016/j.devcel.2008.12.004.Peer-Reviewed Original Research
2008
Chapter 4 Protein Trafficking in Polarized Cells
Duffield A, Caplan MJ, Muth TR. Chapter 4 Protein Trafficking in Polarized Cells. International Review Of Cytology 2008, 270: 145-179. PMID: 19081536, DOI: 10.1016/s1937-6448(08)01404-4.Peer-Reviewed Original ResearchConceptsEpithelial cellsProtein traffickingBasolateral membrane surfaceLipid traffickingPolarized cellsDynamic regulationSpecific lipidsAdjacent epithelial cellsCell typesBasolateral surfaceApical surfaceCertain cellsMembrane surfaceTraffickingProtein contentCellsSortingNumber of sortingsImmune systemRecent advancesMechanismProteinRegulationEpitheliumLipids
2007
Arrestins and Spinophilin Competitively Regulate Na+,K+-ATPase Trafficking through Association with a Large Cytoplasmic Loop of the Na+,K+-ATPase
Kimura T, Allen PB, Nairn AC, Caplan MJ. Arrestins and Spinophilin Competitively Regulate Na+,K+-ATPase Trafficking through Association with a Large Cytoplasmic Loop of the Na+,K+-ATPase. Molecular Biology Of The Cell 2007, 18: 4508-4518. PMID: 17804821, PMCID: PMC2043564, DOI: 10.1091/mbc.e06-08-0711.Peer-Reviewed Original ResearchMeSH Keywords14-3-3 ProteinsAnimalsArrestinBinding, CompetitiveCell LineChlorocebus aethiopsChoroid PlexusCytoplasmG-Protein-Coupled Receptor KinasesKidneyMiceMicrofilament ProteinsNerve Tissue ProteinsPhosphorylationProtein BindingProtein SubunitsProtein TransportRabbitsSodium-Potassium-Exchanging ATPaseConceptsG protein-coupled receptorsLarge cytoplasmic loopExpression of spinophilinCytoplasmic loopMock-transfected cellsGRK-2Adrenergic hormonesReceptor signalingImportant modulatorSpinophilinATPase endocytosisATPase traffickingArrestin-2COS cellsArrestinHormoneAssociationATPaseGRKsCellsTraffickingEpsilonVasopressinReceptorsTransport protein sorting in polarized epithelial cells.
Zhang L, Caplan MJ. Transport protein sorting in polarized epithelial cells. Acta Physiol Sinica 2007, 59: 505-11. PMID: 17700970.Peer-Reviewed Original ResearchConceptsTransport proteinsMembrane transport proteinsPolarized epithelial cellsProtein-protein interactionsCellular energy sensorEpithelial cellsCell surface domainsCell-matrix contactsSurface domainsPlasma membraneEnergy sensorPhysiological functionsDistinct domainsExquisite organizationPolarized domainsJunctional complexesProteinEpithelial tissuesCellsCascadeParacellular pathwayRecent evidenceDomainKinaseDifferent collectionsTetraspan 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 propertiesCellsThe Future of the Pump
Caplan MJ. The Future of the Pump. Journal Of Clinical Gastroenterology 2007, 41: s217-s222. PMID: 17575526, DOI: 10.1097/mcg.0b013e31803233da.Peer-Reviewed Original ResearchConceptsIon transport proteinsLarge macromolecular complexesMacromolecular complexesGastric parietal cellsTransport proteinsSecond messengerMacromolecular interactionsIon translocationRegulatory processesK-ATPaseCritical roleTight controlX-ray crystallographic techniquesParietal cellsCrystallographic techniquesCellsKinasePharmacologic suppressionTraffickingProteinTranslocationMessengerMolecular structureRegulationSecretion
2006
AMP-activated protein kinase regulates the assembly of epithelial tight junctions
Zhang L, Li J, Young LH, Caplan MJ. AMP-activated protein kinase regulates the assembly of epithelial tight junctions. Proceedings Of The National Academy Of Sciences Of The United States Of America 2006, 103: 17272-17277. PMID: 17088526, PMCID: PMC1859922, DOI: 10.1073/pnas.0608531103.Peer-Reviewed Original ResearchConceptsTight junction assemblyJunction assemblyProtein kinaseLKB1-dependent phosphorylationCell polarization processCellular energy statusActivation of AMPKTight junctionsEukaryotic cellsTight junction structureAMPKMDCK cellsEpithelial tight junctionsEnergy statusKinaseEpithelial cellsAbsence of Ca2AssemblyTransepithelial electrical resistanceParacellular fluxZonula occludens-1CellsRecent studiesOccludens-1LKB1
2004
Gastric parietal cell acid secretion in mice can be regulated independently of H+/K+ ATPase endocytosis
Nguyen NV, Gleeson PA, Courtois-Coutry N, Caplan MJ, van Driel IR. Gastric parietal cell acid secretion in mice can be regulated independently of H+/K+ ATPase endocytosis. Gastroenterology 2004, 127: 145-154. PMID: 15236181, DOI: 10.1053/j.gastro.2004.04.016.Peer-Reviewed Original ResearchConceptsApical plasma membranePlasma membraneIntracellular traffickingTyrosine-based endocytosis motifATPase activityATPase beta subunitMembrane traffickingATPase endocytosisTrafficking eventsEndocytosis motifParietal cell ultrastructureTubulovesicular compartmentCytoplasmic tailIntracytoplasmic compartmentCl- conductanceParietal cell acid secretionBeta subunitParietal cellsDirect regulationProton pumpCell ultrastructureTraffickingATPaseCellsRegulationSorting 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