2023
The C-terminal tail of polycystin-1 suppresses cystic disease in a mitochondrial enzyme-dependent fashion
Onuchic L, Padovano V, Schena G, Rajendran V, Dong K, Shi X, Pandya R, Rai V, Gresko N, Ahmed O, Lam T, Wang W, Shen H, Somlo S, Caplan M. The C-terminal tail of polycystin-1 suppresses cystic disease in a mitochondrial enzyme-dependent fashion. Nature Communications 2023, 14: 1790. PMID: 36997516, PMCID: PMC10063565, DOI: 10.1038/s41467-023-37449-1.Peer-Reviewed Original ResearchConceptsPolycystin-1Nicotinamide nucleotide transhydrogenaseTerminal tailCystic phenotypeAutosomal dominant polycystic kidney diseaseCyst cell proliferationC-terminal domainAmino acid residuesLethal monogenic disorderC-terminal cleavageNucleotide transhydrogenaseAcid residuesMitochondrial functionTransgenic expressionPKD1 geneRedox stateShort fragmentsCell proliferationMonogenic disordersDominant polycystic kidney diseasePolycystic kidney diseaseGene therapy strategiesProteinPhenotypeFragments
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
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 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 blockTraffickingProteinMembraneCells
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
2011
Renal 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 alterationsRegulated 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
Association with β-COP Regulates the Trafficking of the Newly Synthesized Na,K-ATPase*
Morton MJ, Farr GA, Hull M, Capendeguy O, Horisberger JD, Caplan MJ. Association with β-COP Regulates the Trafficking of the Newly Synthesized Na,K-ATPase*. Journal Of Biological Chemistry 2010, 285: 33737-33746. PMID: 20801885, PMCID: PMC2962472, DOI: 10.1074/jbc.m110.141119.Peer-Reviewed Original ResearchConceptsK-ATPase αK-ATPase β-subunitΒ-COPΒ-subunitΑ-subunitPlasma membraneEndoplasmic reticulumK-ATPase α-subunitMutant α-subunitsIon-transporting ATPasePlasma membrane expressionK-ATPasePulse-chase experimentsPartner proteinsNovel labeling techniqueCoat proteinDibasic motifCell surfaceMembrane expressionObligate intermediateΒ subunit expressionProteinReticulumVisualizing 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 ResearchRenal Cystic Proteins in the Olfactory Epithelium (OE)
Pluznick J, Rodriguez‐Gil D, Hull M, Mistry K, Gattone V, Johnson C, Weatherbee S, Greer C, Caplan M. Renal Cystic Proteins in the Olfactory Epithelium (OE). The FASEB Journal 2010, 24: 1002.17-1002.17. DOI: 10.1096/fasebj.24.1_supplement.1002.17.Peer-Reviewed Original ResearchMutant animalsPolycystin-2Olfactory epitheliumIndividual olfactory receptorsDisease-causing mutationsCilia formationΑ-tubulin stainingMurine olfactory epitheliumMature olfactory neuronsMKS3Olfactory receptorsOlfactory neuronsProteinDendritic knobsCiliaPhysiological activityMutant miceAC3 expressionVitro dataMutant ratsRT-PCRSyndrome 1Similar reductionExpressionRatsPolarized traffic towards the cell surface: how to find the route
Carmosino M, Valenti G, Caplan M, Svelto M. Polarized traffic towards the cell surface: how to find the route. Biology Of The Cell 2010, 102: 75-91. PMID: 19909237, DOI: 10.1042/bc20090134.Peer-Reviewed Original Research
2009
Chapter 11 Detecting the Surface Localization and Cytoplasmic Cleavage of Membrane-Bound Proteins
Chapin HC, Rajendran V, Capasso A, Caplan MJ. Chapter 11 Detecting the Surface Localization and Cytoplasmic Cleavage of Membrane-Bound Proteins. Methods In Cell Biology 2009, 94: 223-239. PMID: 20362093, PMCID: PMC3063071, DOI: 10.1016/s0091-679x(08)94011-5.Peer-Reviewed Original ResearchConceptsC-terminal tailPolycystin-1Membrane-bound proteinsSubcellular localizationNuclear localizationPlasma membranePC1 proteinCytoplasmic cleavagePhysiological functionsSurface localizationFunctional roleSurface proteinsCell surfaceSurface populationsSpecific cleavageProteinImmunofluorescence protocolSoluble fragmentProtein expressionCell populationsImportant poolAutosomal dominant polycystic kidney diseasePolycystic kidney diseaseCleavageComplete understandingMembrane 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 membraneGolgiPathwayCellsMembraneGTPasesLocalization of proteins associated with renal cystic diseases to the olfactory epithelium
Pluznick J, Rodriguez‐Gil D, Mistry K, Hull M, Johnson C, Greer C, Caplan M. Localization of proteins associated with renal cystic diseases to the olfactory epithelium. The FASEB Journal 2009, 23: 796.11-796.11. DOI: 10.1096/fasebj.23.1_supplement.796.11.Peer-Reviewed Original Research
2008
The Cytoplasmic Tail Dileucine Motif LL572 Determines the Glycosylation Pattern of Membrane-type 1 Matrix Metalloproteinase*
Ludwig T, Theissen SM, Morton MJ, Caplan MJ. The Cytoplasmic Tail Dileucine Motif LL572 Determines the Glycosylation Pattern of Membrane-type 1 Matrix Metalloproteinase*. Journal Of Biological Chemistry 2008, 283: 35410-35418. PMID: 18955496, PMCID: PMC2602891, DOI: 10.1074/jbc.m801816200.Peer-Reviewed Original ResearchConceptsMT1-MMPMT1-MMP traffickingSite-directed mutagenesis studiesCell surface traffickingMembrane type 1 matrix metalloproteinasePost-translational processingCytoplasmic tailMolecular charactersMutagenesis studiesSurface traffickingMetabolic labelingSubstrate spectrumMatrix metalloproteinaseEnzymatic deglycosylationGlycosylation patternsProfound physiological effectsHinge regionTraffickingPathological processesProteinLectin precipitationPost-synthetic pathwayPhysiological effectsMajor effectBroad spectrumEpithelial junctions and polarity: complexes and kinases
Caplan MJ, Seo-Mayer P, Zhang L. Epithelial junctions and polarity: complexes and kinases. Current Opinion In Nephrology & Hypertension 2008, 17: 506-512. PMID: 18695392, PMCID: PMC3057677, DOI: 10.1097/mnh.0b013e32830baaae.Peer-Reviewed Original ResearchConceptsEpithelial cell polarityCell polarityEpithelial cell polarizationJunctional complexesIntercellular adhesion junctionsImportant physiological ramificationsCalcium-dependent adhesion proteinCell-cell contactCellular energy metabolismProtein complexesMembrane proteinsAdhesion junctionsPlasmalemmal domainsAdhesion proteinsCell polarizationPhysiological ramificationsEpithelial junctionsKinaseEnergy metabolismCharacteristic polarityEpithelial cellsProteinParacellular permeabilityNovel classComplexesChapter 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
Transport 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 collections