2015
Dual 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
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 alterations
2010
Polycystin-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
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 ResearchMeSH KeywordsAnimalsCell LineCell MembraneCytoplasmEnzyme-Linked Immunosorbent AssayFluorescent Antibody TechniqueGenes, ReporterHumansLuciferasesMembrane ProteinsRecombinant Fusion ProteinsTRPP Cation ChannelsConceptsC-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 understanding
2006
An Extracellular Loop of the Human Non-Gastric H,K-ATPase a-subunit is Involved in Apical Plasma Membrane Polarization
Lerner M, Lemke D, Bertram H, Schillers H, Oberleithner H, Caplan MJ, Reinhardt J. An Extracellular Loop of the Human Non-Gastric H,K-ATPase a-subunit is Involved in Apical Plasma Membrane Polarization. Cellular Physiology And Biochemistry 2006, 18: 75-84. PMID: 16914892, DOI: 10.1159/000095169.Peer-Reviewed Original ResearchConceptsP-type ATPasesSorting motifApical deliveryExtracellular loopK-ATPaseSpecific sorting signalsPlasma membrane polarizationShort extracellular loopApical plasma membraneMadin-Darby canine kidney cellsSingle point mutationCanine kidney cellsSorting signalsGene familyPlasma membraneFlanking regionsEpithelial apical membraneK-ATPasesPhysiological roleApical membraneCellular distributionPoint mutationsIon pumpsATP1AL1Corresponding region
2000
Differential localization of human nongastric H+-K+-ATPase ATP1AL1 in polarized renal epithelial cells
Reinhardt J, Grishin A, Oberleithner H, Caplan M. Differential localization of human nongastric H+-K+-ATPase ATP1AL1 in polarized renal epithelial cells. American Journal Of Physiology. Renal Physiology 2000, 279: f417-f425. PMID: 10966921, DOI: 10.1152/ajprenal.2000.279.3.f417.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCell PolarityEpithelial CellsFluorescent Antibody TechniqueGene Expression Regulation, EnzymologicH(+)-K(+)-Exchanging ATPaseHumansKidneyLLC-PK1 CellsMicroscopy, ConfocalStomachSwineTransfectionConceptsApical plasma membranePlasma membraneRenal epithelial cellsIon pumpsPlasma membrane localizationConfocal immunofluorescence microscopyEpithelial cellsATPase beta subunitRenal epithelial cell lineMembrane localizationLow expression levelsEpithelial cell lineSurface biotinylationPump subunitsBeta subunitFunctional expressionStable transfectionLateral membranesMDCK cellsATP1AL1Immunofluorescence microscopyDifferential localizationSorting mechanismStable interactionExpression levels
1998
Identification of Sorting Determinants in the C-terminal Cytoplasmic Tails of the γ-Aminobutyric Acid Transporters GAT-2 and GAT-3*
Muth T, Ahn J, Caplan M. Identification of Sorting Determinants in the C-terminal Cytoplasmic Tails of the γ-Aminobutyric Acid Transporters GAT-2 and GAT-3*. Journal Of Biological Chemistry 1998, 273: 25616-25627. PMID: 9748227, DOI: 10.1074/jbc.273.40.25616.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBiological TransportCarrier ProteinsCells, CulturedCloning, MolecularDogsFluorescent Antibody TechniqueGABA Plasma Membrane Transport ProteinsGamma-Aminobutyric AcidGenes, mycIon ChannelsKidneyMembrane ProteinsMembrane Transport ProteinsMicroscopy, ConfocalMolecular Sequence DataRecombinant Fusion ProteinsSequence DeletionConceptsC-terminal cytoplasmic tailIon transport proteinsMadin-Darby canine kidney cellsCytoplasmic tailMembrane proteinsC-terminusCanine kidney cellsTransporter familyAmino acidsBasolateral distributionTransport proteinsGAT-2Polytopic membrane proteinsProtein-based signalsProtein-protein interactionsTerminal cytoplasmic tailC-terminal sequencesKidney cellsClass of polypeptidesEpithelial cellsApical sortingPDZ domainChimeric transportersPolarized sortingSorting determinant
1997
Low-flow ischemia leads to translocation of canine heart GLUT-4 and GLUT-1 glucose transporters to the sarcolemma in vivo.
Young L, Renfu Y, Russell R, Hu X, Caplan M, Ren J, Shulman G, Sinusas A. Low-flow ischemia leads to translocation of canine heart GLUT-4 and GLUT-1 glucose transporters to the sarcolemma in vivo. Circulation 1997, 95: 415-22. PMID: 9008459, DOI: 10.1161/01.cir.95.2.415.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBiological TransportDogsFluorescent Antibody TechniqueGlucose Transporter Type 1Glucose Transporter Type 4HeartIntracellular MembranesMonosaccharide Transport ProteinsMuscle ProteinsMyocardial IschemiaMyocardiumRegional Blood FlowSarcolemmaSubcellular FractionsTissue Distribution
1994
The axonal gamma-aminobutyric acid transporter GAT-1 is sorted to the apical membranes of polarized epithelial cells.
Pietrini G, Suh YJ, Edelmann L, Rudnick G, Caplan MJ. The axonal gamma-aminobutyric acid transporter GAT-1 is sorted to the apical membranes of polarized epithelial cells. Journal Of Biological Chemistry 1994, 269: 4668-4674. PMID: 8308038, DOI: 10.1016/s0021-9258(17)41828-x.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAxonsBetaineCarrier ProteinsCell CompartmentationCell LineCell MembraneCell PolarityCells, CulturedDogsEpitheliumFluorescent Antibody TechniqueGABA Plasma Membrane Transport ProteinsGamma-Aminobutyric AcidIn Vitro TechniquesMembrane ProteinsMembrane Transport ProteinsNerve Tissue ProteinsOrganic Anion TransportersConceptsGamma-aminobutyric acid (GABA) transporter GAT-1MDCK cellsDistinct cell surface domainsEpithelial Madin-Darby canine kidney (MDCK) cell lineTransporter GAT-1Cell surfaceCell surface domainsCell surface biotinylationApical cell surfaceBasolateral cell surfaceEpithelial cellsBGT-1Axonal plasma membraneCell surface membraneSorting signalsCanine kidney cell lineMadin-Darby canine kidney (MDCK) cell lineGAT-1GABA transporterDistinct subdomainsKidney cell lineBetaine transporterHyperosmotic stressSurface biotinylationApical localization
1992
Isoforms of the Na,K-ATPase are present in both axons and dendrites of hippocampal neurons in culture.
Pietrini G, Matteoli M, Banker G, Caplan MJ. Isoforms of the Na,K-ATPase are present in both axons and dendrites of hippocampal neurons in culture. Proceedings Of The National Academy Of Sciences Of The United States Of America 1992, 89: 8414-8418. PMID: 1326755, PMCID: PMC49930, DOI: 10.1073/pnas.89.18.8414.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAxonsCell PolarityCells, CulturedDendritesEpitheliumFluorescent Antibody TechniqueHippocampusIn Vitro TechniquesIsoenzymesRatsSodium-Potassium-Exchanging ATPaseTransfectionConceptsHippocampal neuronsAlpha 1Epithelial cellsMature cultured hippocampal neuronsCultured hippocampal neuronsK-ATPase alpha subunitPolarized epithelial cell lineAlpha 3 proteinAlpha 3 isoformDistribution of isoformsEpithelial cell lineRenal epithelial cellsInfluenza glycoproteinsVesicular stomatitis virusNeuronal cellsNeuronsAlpha subunitCell linesStable transfectionStomatitis virusAxonsK-ATPaseIsoformsCellsDendrites
1988
Immunocytochemical localization of plasmalemmal proteins in semi-thin sections of epithelial monolayers.
Smith ZD, Caplan MJ, Jamieson JD. Immunocytochemical localization of plasmalemmal proteins in semi-thin sections of epithelial monolayers. Journal Of Histochemistry & Cytochemistry 1988, 36: 311-316. PMID: 2449492, DOI: 10.1177/36.3.2449492.Peer-Reviewed Original Research
1987
Localization of Na+,K+-ATPase alpha-subunit to the sinusoidal and lateral but not canalicular membranes of rat hepatocytes.
Sztul ES, Biemesderfer D, Caplan MJ, Kashgarian M, Boyer JL. Localization of Na+,K+-ATPase alpha-subunit to the sinusoidal and lateral but not canalicular membranes of rat hepatocytes. Journal Of Cell Biology 1987, 104: 1239-1248. PMID: 3032985, PMCID: PMC2114466, DOI: 10.1083/jcb.104.5.1239.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCell MembraneFluorescent Antibody TechniqueHistocytochemistryIn Vitro TechniquesLiverMacromolecular SubstancesMicroscopy, ElectronRatsSodium-Potassium-Exchanging ATPaseConceptsAlpha-subunit bandsRat liver plasma membrane fractionsPlasma membraneAlpha subunitCatalytic activityMembrane fractionEntire plasma membranePlasma membrane fractionATPase alpha subunitIon-transporting epitheliaMonoclonal antibodiesWestern blotLiver plasma membrane fractionsBasolateral domainBasolateral distributionPolyclonal antibodies
1985
Monoclonal antibody to Na,K-ATPase: Immunocytochemical localization along nephron segments
Kashgarian M, Biemesderfer D, Caplan M, Forbush B. Monoclonal antibody to Na,K-ATPase: Immunocytochemical localization along nephron segments. Kidney International 1985, 28: 899-913. PMID: 3003443, DOI: 10.1038/ki.1985.216.Peer-Reviewed Original ResearchConceptsMonoclonal antibodiesNephron segmentsEvidence of labellingRenal tubular epithelial cellsTubular epithelial cellsK-ATPaseThick ascending limbOnly principal cellsDifferent nephron segmentsDog antigensBasal-lateral membranesSignificant antibodiesAscending limbMesangial regionHenle's loopOccasional cellsRenal medullaOuter renal medullaAbundant antibodyAntibodiesApical labelingTubule segmentsPrincipal cellsEpithelial cellsImmunocytochemical localization