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
2020
A cut above (and below): Protein cleavage in the regulation of polycystin trafficking and signaling
Padovano V, Mistry K, Merrick D, Gresko N, Caplan MJ. A cut above (and below): Protein cleavage in the regulation of polycystin trafficking and signaling. Cellular Signalling 2020, 72: 109634. PMID: 32283256, PMCID: PMC7269866, DOI: 10.1016/j.cellsig.2020.109634.Peer-Reviewed Original ResearchConceptsPolycystin-1Polycystin proteinsG proteinsPolycystin-1 proteinProtein maturationTerminal tailObligate stepBiological pathwaysProtein cleavagePhysiological functionsProteolytic siteProteinPathological consequencesAutosomal dominant polycystic kidney diseaseTraffickingDominant polycystic kidney diseasePolycystic kidney diseasePrimary functionCleavageRegulationMaturationGenesMitochondriaValuable insightsPathway
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
2014
Trafficking 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
Polycystin-1 cleavage and the regulation of transcriptional pathways
Merrick D, Bertuccio CA, Chapin HC, Lal M, Chauvet V, Caplan MJ. Polycystin-1 cleavage and the regulation of transcriptional pathways. Pediatric Nephrology 2013, 29: 505-511. PMID: 23824180, PMCID: PMC3844055, DOI: 10.1007/s00467-013-2548-y.Peer-Reviewed Original ResearchConceptsAutosomal dominant polycystic kidney diseaseFluid-filled renal cystsPolycystin-2Transcriptional pathwaysPolycystin-1Primary ciliaProtein productsPhysiological functionsCommon genetic causeParent proteinProteolytic cleavageCleavage fragmentsGenetic causeGenesEnd-stage renal diseaseDominant polycystic kidney diseasePolycystic kidney diseaseBiological activityPathwayRenal diseaseKidney diseaseCleavageRenal parenchymaFragmentsRenal cystsPolycystin-1C terminus cleavage and its relation with polycystin-2, two proteins involved in polycystic kidney disease.
Bertuccio CA, Caplan MJ. Polycystin-1C terminus cleavage and its relation with polycystin-2, two proteins involved in polycystic kidney disease. Medicina 2013, 73: 155-62. PMID: 23570767.Peer-Reviewed Original ResearchConceptsPolycystin-1Polycystin-2Autosomal dominant polycystic kidney diseaseTerminal cytoplasmic tailProtein sortingNormal tubulogenesisPolycystic kidney diseaseProtein functionCytoplasmic tailTerminal tailCommon genetic causeCystogenic processExtracellular matrixDifferentiation mechanismsCellular proliferationGenetic causeMultiple cleavagesDominant polycystic kidney diseasePathwayHigh proliferative rateCleavageProliferative rateSecretory characteristicsGenesTubulogenesis
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
Visualizing 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
2004
Mechanical stimuli induce cleavage and nuclear translocation of the polycystin-1 C terminus
Chauvet V, Tian X, Husson H, Grimm DH, Wang T, Hieseberger T, Igarashi P, Bennett AM, Ibraghimov-Beskrovnaya O, Somlo S, Caplan MJ. Mechanical stimuli induce cleavage and nuclear translocation of the polycystin-1 C terminus. Journal Of Clinical Investigation 2004, 114: 1433-1443. PMID: 15545994, PMCID: PMC525739, DOI: 10.1172/jci21753.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsCell LineCell NucleusChlorocebus aethiopsCHO CellsCOS CellsCricetinaeCricetulusDogsEmbryo, MammalianEpithelial CellsKidney TubulesMembrane ProteinsMiceMice, TransgenicPolycystic Kidney, Autosomal DominantProteinsSequence DeletionSignal TransductionStress, MechanicalTranscription Factor AP-1TRPP Cation ChannelsConceptsC-terminal tailAutosomal dominant polycystic kidney diseaseCell-matrix interactionsCiliary signalingSecond genePolycystin-2Polycystin-1C-terminusNovel pathwayProteolytic cleavageNuclear translocationMechanical stimuliGenesDominant polycystic kidney diseasePolycystic kidney diseasePrecise mechanismCleavageTerminusSignalingTranslocationNucleusPathway
2001
Ion Pumps in Polarized Cells: Sorting and Regulation of the Na+,K+- and H+,K+-ATPases*
Dunbar L, Caplan M. Ion Pumps in Polarized Cells: Sorting and Regulation of the Na+,K+- and H+,K+-ATPases*. Journal Of Biological Chemistry 2001, 276: 29617-29620. PMID: 11404365, DOI: 10.1074/jbc.r100023200.Peer-Reviewed Original ResearchConceptsP-type familyIon transport proteinsDistinct regulatory pathwaysSubcellular localizationPolarized cellsRelated membersRegulatory pathwaysTransport proteinsMolecular signalsATPasesCellular mechanismsIon pumpsEnzymatic activityEpithelial cellsProteinComplex arrayCatalytic capacityPhysiologic functionIntramolecular interactionsCellsHomologyTraffickingATPasePathwayRegulation
2000
The cell biology of ion pumps: sorting and regulation
Dunbar L, Caplan M. The cell biology of ion pumps: sorting and regulation. European Journal Of Cell Biology 2000, 79: 557-563. PMID: 11001492, DOI: 10.1078/0171-9335-00079.Peer-Reviewed Original ResearchConceptsPolarized epithelial cellsP-type familyIon pumpsK-ATPaseDistinct regulatory pathwaysProtein traffickingSubcellular localizationCell biologyRelated membersRegulatory pathwaysMolecular signalsCellular mechanismsEnzymatic activityIntra-molecular interactionsEpithelial cellsTraffickingComplex arrayCatalytic capacityPhysiologic functionATPasesHomologyBiologyPathwayRegulationSorting
1998
Signals and Mechanisms of Sorting in Epithelial Polarity
Gottardi C, Caplan M. Signals and Mechanisms of Sorting in Epithelial Polarity. Advances In Molecular And Cell Biology 1998, 26: 95-131. PMCID: PMC7147917, DOI: 10.1016/s1569-2558(08)60020-x.Peer-Reviewed Original ResearchPolarized epithelial phenotypePlasma membrane domainsCell type controlPolarized epithelial cellsEpithelial membrane polarityEpithelial polarityPolarized organizationCell biologistsIntracellular organellesEpithelial phenotypeCell typesDistinct compartmentsCell physiologistsSemi-permeable barrierIon transport processesEpithelial cellsType controlsOrganismsCellsElectron microscopic levelOrganellesBiologistsFundamental featuresPhenotypePathway
1997
Epithelial Cell Polarity: Challenges and Methodologies
Caplan M, Rodriguez‐Boulan E. Epithelial Cell Polarity: Challenges and Methodologies. 1997, 665-688. DOI: 10.1002/cphy.cp140117.Peer-Reviewed Original ResearchEpithelial polarityProtein trafficking pathwaysEpithelial cell polarityTissue-specific variationsEpithelial cellsSorting machineryProtein polarityCell polaritySorting signalsTargeting pathwaysTrafficking pathwaysRecycling pathwayBiochemical techniquesE-cadherinVitro systemEpithelial monolayersGenetic modelsPathwayBiogenetic pathwayMorphological techniquesCellsPolarityMachinerySubstrataTranscytosisIon pumps in epithelial cells: sorting, stabilization, and polarity
Caplan MJ. Ion pumps in epithelial cells: sorting, stabilization, and polarity. American Journal Of Physiology 1997, 272: g1304-g1313. PMID: 9227464, DOI: 10.1152/ajpgi.1997.272.6.g1304.Peer-Reviewed Original ResearchMembrane polarity in epithelial cells: protein sorting and establishment of polarized domains
Caplan MJ. Membrane polarity in epithelial cells: protein sorting and establishment of polarized domains. American Journal Of Physiology 1997, 272: f425-f429. PMID: 9140041, DOI: 10.1152/ajprenal.1997.272.4.f425.Peer-Reviewed Original ResearchConceptsTransport proteinsEpithelial cellsDistinct surface domainsEpithelial cell typesProtein sortingBiological specializationCellular pathwaysPlasma membranePolarized epitheliumElegant networkMembrane polarityCell typesBasolateral surfaceDistinct populationsProteinBasolateral portionPhysiological propertiesSurface domainsCellsAbsolute prerequisiteDomainPlasmalemmaPathwaySortingMembrane
1995
Na+,K+-ATPase in the Choroid Plexus REGULATION BY SEROTONIN/PROTEIN KINASE C PATHWAY (∗)
Fryckstedt J, Caplan M, Aperia A, Fisone G, Snyder G, Greengard P. Na+,K+-ATPase in the Choroid Plexus REGULATION BY SEROTONIN/PROTEIN KINASE C PATHWAY (∗). Journal Of Biological Chemistry 1995, 270: 2427-2430. PMID: 7852300, DOI: 10.1074/jbc.270.6.2427.Peer-Reviewed Original ResearchConceptsProtein kinase CKinase CTwo-dimensional peptide mappingProtein kinase C pathwayKinase C pathwayProtein phosphorylationFirst messengersIntact cellsIon pumpsPeptide mappingATPaseC pathwayPhosphorylationPhorbolDemonstrated abilityMessengerComigrationActivatorRegulationPathwayActivityChoroid plexusMechanismProductionTurnover
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 secretionIntegrinsVesiclesLamininPathwayMembraneCells