2008
Polycystin-1 C-terminal tail associates with β-catenin and inhibits canonical Wnt signaling
Lal M, Song X, Pluznick JL, Di Giovanni V, Merrick DM, Rosenblum ND, Chauvet V, Gottardi CJ, Pei Y, Caplan MJ. Polycystin-1 C-terminal tail associates with β-catenin and inhibits canonical Wnt signaling. Human Molecular Genetics 2008, 17: 3105-3117. PMID: 18632682, PMCID: PMC2722884, DOI: 10.1093/hmg/ddn208.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBeta CateninBinding SitesCell LineCell NucleusCHO CellsCricetinaeCricetulusGene Expression ProfilingGene Expression RegulationHumansLigandsOligonucleotide Array Sequence AnalysisPeptide FragmentsPolycystic Kidney, Autosomal DominantRecombinant ProteinsSignal TransductionSystems BiologyTCF Transcription FactorsTransfectionTRPP Cation ChannelsWnt ProteinsConceptsC-terminal tailCanonical WntPolycystin-1Wnt-dependent signalingDNA microarray analysisDependent gene transcriptionN-terminal portionInhibits canonical WntTCF proteinsT-cell factorAutosomal dominant polycystic kidney disease (ADPKD) casesMotif presentGene transcriptionDevelopmental processesMicroarray analysisWntPKD1 geneΒ-cateninNovel mechanism
2005
The C-Terminal Tail of the Polycystin-1 Protein Interacts with the Na,K-ATPase α-Subunit
Zatti A, Chauvet V, Rajendran V, Kimura T, Pagel P, Caplan MJ. The C-Terminal Tail of the Polycystin-1 Protein Interacts with the Na,K-ATPase α-Subunit. Molecular Biology Of The Cell 2005, 16: 5087-5093. PMID: 16107561, PMCID: PMC1266409, DOI: 10.1091/mbc.e05-03-0200.Peer-Reviewed Original ResearchConceptsC-terminal tailPolycystin-1Cytoplasmic C-terminal tailK-ATPase α-subunitPolycystin-1 proteinK-ATPase activityRegulation of NaChinese hamster ovary cellsProtein interactsHamster ovary cellsProtein exhibitΑ-subunitFunctional studiesAmino acidsPKD1 geneOvary cellsAutosomal dominant polycystic kidney diseaseDominant polycystic kidney diseasePolycystic kidney diseaseInteractsKinetic propertiesRegulationGenesTailProtein
2003
The tetraspanin CD63 enhances the internalization of the H,K-ATPase β-subunit
Duffield A, Kamsteeg EJ, Brown AN, Pagel P, Caplan MJ. The tetraspanin CD63 enhances the internalization of the H,K-ATPase β-subunit. Proceedings Of The National Academy Of Sciences Of The United States Of America 2003, 100: 15560-15565. PMID: 14660791, PMCID: PMC307607, DOI: 10.1073/pnas.2536699100.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAntigens, CDChlorocebus aethiopsCloning, MolecularCOS CellsGene LibraryH(+)-K(+)-Exchanging ATPaseHumansKidneyMembrane ProteinsModels, BiologicalPlatelet Membrane GlycoproteinsProtein SubunitsProtein TransportRabbitsRatsRats, Sprague-DawleyRecombinant ProteinsTetraspanin 30TransfectionConceptsAdaptor protein complex 2Intracellular compartmentsK-ATPaseTetraspanin CD63K-ATPase β-subunitCOS-7 cellsEndocytic machineryAdaptor proteinLate endosomesSecretory vesiclesPlasma membraneGastric parietal cellsBiochemical experimentsInteraction partnersΒ-subunitParietal cellsCell surfaceEnhanced endocytosisTubulovesicular elementsCD63CompartmentsCellsInternalizationComplexes 2Endosomes
2000
The Roles of Carbohydrate Chains of the β-Subunit on the Functional Expression of Gastric H+,K+-ATPase*
Asano S, Kawada K, Kimura T, Grishin A, Caplan M, Takeguchi N. The Roles of Carbohydrate Chains of the β-Subunit on the Functional Expression of Gastric H+,K+-ATPase*. Journal Of Biological Chemistry 2000, 275: 8324-8330. PMID: 10722662, DOI: 10.1074/jbc.275.12.8324.Peer-Reviewed Original ResearchConceptsAlpha/beta assemblyN-glycosylation sitesATPase activityBeta assemblyPutative N-glycosylation sitesCarbohydrate chainsAlpha/beta complexSingle carbohydrate chainCatalytic subunitSurface deliveryFunctional enzymeAsparagine residuesAlpha subunitΒ-subunitBeta complexDelivery mechanismFunctional expressionComplete lossATPaseAssemblyExpressionSubunits
1998
ATP1AL1, a Member of the Non-gastric H,K-ATPase Family, Functions as a Sodium Pump*
Grishin A, Caplan M. ATP1AL1, a Member of the Non-gastric H,K-ATPase Family, Functions as a Sodium Pump*. Journal Of Biological Chemistry 1998, 273: 27772-27778. PMID: 9774385, DOI: 10.1074/jbc.273.43.27772.Peer-Reviewed Original Research[25] Expression of neurotransmitter transport systems in polarized cells
Ahn J, Pietrini G, Muth TR, Caplan MJ. [25] Expression of neurotransmitter transport systems in polarized cells. Methods In Enzymology 1998, 296: 370-388. PMID: 9779461, DOI: 10.1016/s0076-6879(98)96027-x.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCarrier ProteinsCell Culture TechniquesCell DivisionCell LineCell MembraneCell PolarityCells, CulturedClone CellsDogsEpithelial CellsGABA Plasma Membrane Transport ProteinsGamma-Aminobutyric AcidHippocampusKidneyMembrane ProteinsMembrane Transport ProteinsNeuronsOrganic Anion TransportersRecombinant ProteinsTransfectionConceptsNeurotransmitter transport systemsComplementary DNASpecific subcellular distributionTransport protein familySpecific subcellular structuresExogenous protein expressionCultured epithelial cell linesProtein familyEpithelial cell linePlasma membraneTransport assaysTransport proteinsTransporter proteinsSubcellular distributionSubcellular structuresTransport systemFluorescence microscopySpecific subdomainsProtein expressionCell linesProteinExpressionCellsTransportersDNA
1997
A Tyrosine-Based Signal Targets H/K-ATPase to a Regulated Compartment and Is Required for the Cessation of Gastric Acid Secretion
Courtois-Coutry N, Roush D, Rajendran V, McCarthy J, Geibel J, Kashgarian M, Caplan M. A Tyrosine-Based Signal Targets H/K-ATPase to a Regulated Compartment and Is Required for the Cessation of Gastric Acid Secretion. Cell 1997, 90: 501-510. PMID: 9267030, DOI: 10.1016/s0092-8674(00)80510-3.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCalciumCOS CellsCytomegalovirusDNA PrimersEndocytosisGastric AcidGastric MucosaH(+)-K(+)-Exchanging ATPaseMacromolecular SubstancesMiceMice, TransgenicMicroscopy, ImmunoelectronMutagenesis, Site-DirectedParietal Cells, GastricPolymerase Chain ReactionPromoter Regions, GeneticRecombinant ProteinsSignal TransductionTransfectionTyrosineConceptsK-ATPase beta subunitTyrosine-based signalsK-ATPaseTyrosine-based endocytosis signalTyrosine residuesBeta subunitIntracellular storage compartmentEndocytosis signalCytoplasmic tailMutant betaRegulated compartmentsSecrete acidResidue sequenceStorage compartmentCell surfaceCell plasmalemmaSubunitsTransgenic miceParietal cellsGastric glandsCompartmentsSecretionAcid secretionReinternalizationPlasmalemmaSorting of Two Polytopic Proteins, the γ-Aminobutyric Acid and Betaine Transporters, in Polarized Epithelial Cells*
Perego C, Bulbarelli A, Longhi R, Caimi M, Villa A, Caplan M, Pietrini G. Sorting of Two Polytopic Proteins, the γ-Aminobutyric Acid and Betaine Transporters, in Polarized Epithelial Cells*. Journal Of Biological Chemistry 1997, 272: 6584-6592. PMID: 9045687, DOI: 10.1074/jbc.272.10.6584.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBiological TransportCarrier ProteinsCell CompartmentationCell LineCell MembraneCell PolarityCytosolDogsEndoplasmic ReticulumFluorescent Antibody Technique, IndirectGABA Plasma Membrane Transport ProteinsHumansMembrane ProteinsMembrane Transport ProteinsMolecular Sequence DataOrganic Anion TransportersReceptors, Nerve Growth FactorRecombinant Fusion ProteinsRecombinant ProteinsStructure-Activity RelationshipTransfectionConceptsCytosolic tailMadin-Darby canine kidney cellsCanine kidney cellsBetaine transporterEndoplasmic reticulumPolarized epithelial cellsTerminal cytosolic domainHuman nerve growth factor receptorKidney cellsPolytopic proteinsApical proteinsCytosolic domainChimeric transportersGrowth factor receptorApical localizationBasolateral distributionBasic residuesBasolateral localizationTransporter isoformsGAT-1Nerve growth factor receptorBgtBasolateral surfaceFactor receptorProteinCloned Catecholamine Transporters Expressed in Polarized Epithelial Cells: Sorting, Drug Sensitivity, and Ion-Coupling Stoichiometry
Gu H, Caplan MJ, Rudnick G. Cloned Catecholamine Transporters Expressed in Polarized Epithelial Cells: Sorting, Drug Sensitivity, and Ion-Coupling Stoichiometry. Advances In Pharmacology 1997, 42: 175-179. PMID: 9327872, DOI: 10.1016/s1054-3589(08)60721-8.Peer-Reviewed Original ResearchMeSH KeywordsAmphetamineAnimalsBiological TransportCarrier ProteinsCell LineCell PolarityCloning, MolecularDopamineDopamine Plasma Membrane Transport ProteinsEpithelial CellsGABA Plasma Membrane Transport ProteinsGamma-Aminobutyric AcidHumansKineticsMembrane GlycoproteinsMembrane ProteinsMembrane Transport ProteinsNerve Tissue ProteinsNorepinephrineNorepinephrine Plasma Membrane Transport ProteinsOrganic Anion TransportersRatsRecombinant Fusion ProteinsRecombinant ProteinsSerotoninSerotonin Plasma Membrane Transport ProteinsSubstrate SpecificitySwineSymportersTransfectionConceptsCell linesPolarized epithelial cellsHeterologous expression systemBiogenic amine transportersCanine kidney cellsSame cellular backgroundKidney cell lineLLC-PK1 cellsExpression systemBiogenic amine releaseCellular backgroundIntact cellsPig kidney cell lineSame cDNAInhibitor sensitivityAmine transportersCatecholamine transportersCoupling stoichiometryTransportersKidney cellsDrug sensitivityPharmacological propertiesEpithelial cellsMolecule of substrateAmine release
1996
Cell-specific Sorting of Biogenic Amine Transporters Expressed in Epithelial Cells*
Gu H, Ahn J, Caplan M, Blakely R, Levey A, Rudnick G. Cell-specific Sorting of Biogenic Amine Transporters Expressed in Epithelial Cells*. Journal Of Biological Chemistry 1996, 271: 18100-18106. PMID: 8663573, DOI: 10.1074/jbc.271.30.18100.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBiogenic AminesBiological TransportCarrier ProteinsCell CompartmentationCell MembraneCell PolarityCells, CulturedDogsDopamineDopamine Plasma Membrane Transport ProteinsEpithelial CellsHumansImmunohistochemistryMembrane GlycoproteinsMembrane Transport ProteinsNerve Tissue ProteinsNorepinephrineNorepinephrine Plasma Membrane Transport ProteinsRatsRecombinant ProteinsSerotoninSerotonin Plasma Membrane Transport ProteinsSymportersConceptsMadin-Darby canine kidneyMDCK cellsLLC-PK1 cellsNeurotransmitter transportersCell surface biotinylationConfocal immunofluorescence microscopyBasolateral membraneCell-specific mechanismsEpithelial cellsBiogenic amine transportersMembrane proteinsSurface biotinylationCDNA encodingHuman DA transporterAmine transportersImmunofluorescence microscopyBiotinylating reagentTransportersPermeable filter supportsApical surfaceImmunocytochemistry resultsBasolateral mediumSurface expressionApical sideDA transporter