2022
Polycystin-2 in the Endoplasmic Reticulum: Bending Ideas about the Role of the Cilium
Caplan MJ. Polycystin-2 in the Endoplasmic Reticulum: Bending Ideas about the Role of the Cilium. Journal Of The American Society Of Nephrology 2022, 33: 1433-1434. PMID: 35906088, PMCID: PMC9342637, DOI: 10.1681/asn.2022050557.Peer-Reviewed Original Research
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 spotsCellsTrafficking
2014
Chemical and Physical Sensors in the Regulation of Renal Function
Pluznick JL, Caplan MJ. Chemical and Physical Sensors in the Regulation of Renal Function. Clinical Journal Of The American Society Of Nephrology 2014, 10: 1626-1635. PMID: 25280495, PMCID: PMC4559500, DOI: 10.2215/cjn.00730114.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 mice
2011
Polycystin-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 cellsRenal Cystic Disease Proteins Play Critical Roles in the Organization of the Olfactory Epithelium
Pluznick JL, Rodriguez-Gil DJ, Hull M, Mistry K, Gattone V, Johnson CA, Weatherbee S, Greer CA, Caplan MJ. Renal Cystic Disease Proteins Play Critical Roles in the Organization of the Olfactory Epithelium. PLOS ONE 2011, 6: e19694. PMID: 21614130, PMCID: PMC3094399, DOI: 10.1371/journal.pone.0019694.Peer-Reviewed Original ResearchConceptsRenal cystic diseaseOlfactory sensory neuronsOlfactory epitheliumCystic diseaseMutant animalsMature olfactory sensory neuronsMurine olfactory epitheliumDendritic knobsOlfactory adenylate cyclaseReceptor expressionSensory neuronsTransduction cascadeLaminar organizationDisease proteinMicrotubule architectureMKS1Syndrome 1Reduced expressionAdenylate cyclaseRT-PCRMKS3DiseaseProteinPhysiological activityObvious alterations
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 ciliaCystsParenchymaPolycystin-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 channels