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 cells
2010
MAL/VIP17, a New Player in the Regulation of NKCC2 in the Kidney
Carmosino M, Rizzo F, Procino G, Basco D, Valenti G, Forbush B, Schaeren-Wiemers N, Caplan MJ, Svelto M. MAL/VIP17, a New Player in the Regulation of NKCC2 in the Kidney. Molecular Biology Of The Cell 2010, 21: 3985-3997. PMID: 20861303, PMCID: PMC2982131, DOI: 10.1091/mbc.e10-05-0456.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBlotting, WesternCell LineEndocytosisEpithelial CellsHumansImmunoprecipitationKidneyLLC-PK1 CellsMembrane Transport ProteinsMiceMice, TransgenicMyelin and Lymphocyte-Associated Proteolipid ProteinsMyelin ProteinsPhosphorylationProtein BindingProteolipidsRatsRats, Inbred WKYRNA InterferenceSodium-Potassium-Chloride SymportersSolute Carrier Family 12, Member 1SwineConceptsRegulation of NKCC2Apical membraneMajor salt transport pathwayC-terminal tailCell surface retentionApical sortingPorcine kidney cellsCotransporter phosphorylationTransgenic mice resultsNephron structuresRegulated absorptionImportant roleNew playersKidney cellsSurface expressionMice resultsSurface retentionTransport pathwaysNKCC2MembraneRegulationLymphocyte-associated proteinCyst formationRat kidney medullaColocalize
2004
Sorting of H,K‐ATPase β‐Subunit in MDCK and LLC‐PK1 Cells is Independent of μ1B Adaptin Expression
Duffield A, Fölsch H, Mellman I, Caplan MJ. Sorting of H,K‐ATPase β‐Subunit in MDCK and LLC‐PK1 Cells is Independent of μ1B Adaptin Expression. Traffic 2004, 5: 449-461. PMID: 15117319, DOI: 10.1111/j.1398-9219.2004.00192.x.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Protein Complex mu SubunitsAdaptor Proteins, Vesicular TransportAmino Acid MotifsAnimalsCell LineCytoplasmDogsEpithelial CellsGlutathione TransferaseH(+)-K(+)-Exchanging ATPaseLLC-PK1 CellsMembrane ProteinsProtein SubunitsProtein TransportReceptors, LDLReceptors, TransferrinRecombinant Fusion ProteinsSwineTransfectionTyrosineConceptsLow-density lipoproteinTransferrin receptorBasolateral localizationTyrosine-based motifMDCK cellsB expressionLLC-PK1 cellsEpithelial cellsLipoproteinMadin-Darby canine kidney cellsCertain epithelial cellsReceptorsKidney cellsCanine kidney cellsK-ATPase beta subunitCellsDifferential expressionK-ATPaseBasolateral expressionExpressionApical membraneCurcumin, a Major Constituent of Turmeric, Corrects Cystic Fibrosis Defects
Egan ME, Pearson M, Weiner SA, Rajendran V, Rubin D, Glöckner-Pagel J, Canny S, Du K, Lukacs GL, Caplan MJ. Curcumin, a Major Constituent of Turmeric, Corrects Cystic Fibrosis Defects. Science 2004, 304: 600-602. PMID: 15105504, DOI: 10.1126/science.1093941.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCalciumCalnexinCell LineCell MembraneCricetinaeCurcuminCystic FibrosisCystic Fibrosis Transmembrane Conductance RegulatorElectrolytesEndoplasmic ReticulumGene TargetingGlycosylationHumansIntestinal MucosaIntestinal ObstructionIsoproterenolMembrane PotentialsMiceMice, KnockoutMutationNasal MucosaPolyethylene GlycolsProtein FoldingRectumTransfectionConceptsCystic fibrosis transmembrane conductance regulatorCFTR proteinDeltaF508 cystic fibrosis transmembrane conductance regulatorDeltaF508 CFTR proteinFibrosis transmembrane conductance regulatorTransmembrane conductance regulatorBaby hamster kidney cellsPlasma membraneComplete knockoutConductance regulatorHamster kidney cellsEndoplasmic reticulumCystic fibrosis defectCFTR geneKidney cellsCFTR miceGenesProteinMutationsCommon mutationsHomozygous expressionCurcumin treatmentFunctional appearanceWeight basisRegulator
2003
The COOH-terminal tail of the GAT-2 GABA transporter contains a novel motif that plays a role in basolateral targeting
Brown A, Muth T, Caplan M. The COOH-terminal tail of the GAT-2 GABA transporter contains a novel motif that plays a role in basolateral targeting. American Journal Of Physiology - Cell Physiology 2003, 286: c1071-c1077. PMID: 15075206, DOI: 10.1152/ajpcell.00291.2003.Peer-Reviewed Original ResearchConceptsBasolateral targetingTerminal tailAmino acidsBasolateral distributionPlasma membrane domainsMadin-Darby canine kidney cellsCanine kidney cellsMembrane domainsTransmembrane proteinNovel motifCOOH terminusMolecular signalsAcid transportersGamma-amino butyric acid (GABA) transportersVectorial transportPolar distributionTransportersButyric acid transporterGAT-2Kidney cellsMotifGABA transporterProteinTargetingAsymmetrical distribution
2002
Aquaporin-2: COOH terminus is necessary but not sufficient for routing to the apical membrane
Deen PM, Van Balkom BW, Savelkoul PJ, Kamsteeg EJ, Van Raak M, Jennings ML, Muth TR, Rajendran V, Caplan MJ. Aquaporin-2: COOH terminus is necessary but not sufficient for routing to the apical membrane. American Journal Of Physiology. Renal Physiology 2002, 282: f330-f340. PMID: 11788448, DOI: 10.1152/ajprenal.0168.2001.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAquaporin 1Aquaporin 2Aquaporin 6AquaporinsArginine VasopressinBlood Group AntigensCell CompartmentationCell FractionationCell LineCell MembraneCell Membrane PermeabilityColforsinEndocytosisGene ExpressionHumansKidneyProtein Structure, TertiaryProtein TransportRatsRecombinant Fusion ProteinsVasoconstrictor AgentsWaterConceptsIntracellular vesiclesApical membraneAquaporin-2Wild‐type aquaporin‐2Mammalian water homeostasisMadin-Darby canine kidney cellsCanine kidney cellsAQP2 accumulationPrimary sequenceSame proteinOsmotic water permeabilityApical expressionForskolin treatmentAquaporin-1 (AQP1) water channelWater homeostasisKidney cellsBasolateral membraneVesiclesPlacental alkaline phosphataseMembraneWater channelsDuct cellsAQP1TailCells
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
Sorting 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
Polarized Expression of GABA Transporters in Madin-Darby Canine Kidney Cells and Cultured Hippocampal Neurons (∗)
Ahn J, Mundigl O, Muth T, Rudnick G, Caplan M. Polarized Expression of GABA Transporters in Madin-Darby Canine Kidney Cells and Cultured Hippocampal Neurons (∗). Journal Of Biological Chemistry 1996, 271: 6917-6924. PMID: 8636119, DOI: 10.1074/jbc.271.12.6917.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsAxonsBase SequenceCarrier ProteinsCell LineDNA PrimersDNA, ComplementaryDogsGABA Plasma Membrane Transport ProteinsGamma-Aminobutyric AcidHippocampusKidneyMembrane ProteinsMembrane Transport ProteinsMicroinjectionsMolecular Sequence DataNeuronsOrganic Anion TransportersConceptsMadin-Darby canine kidney cellsCanine kidney cellsMDCK cellsBetaine transporterMembrane protein sortingAmino acid sequence identityApical membraneCell surface biotinylationGAT-2GABA transporterKidney cellsGamma-aminobutyric acid transporterEpithelial cellsProtein sortingGAT-1Polarized neuronsSurface biotinylationSequence identityAcid transportersCultured hippocampal neuronsHippocampal neuronsPolarized expressionCell typesTransporter GAT-1Basolateral surface
1986
Intracellular sorting and polarized cell surface delivery of (Na+,K+)ATPase, an endogenous component of MDCK cell basolateral plasma membranes
Caplan M, Anderson H, Palade G, Jamieson J. Intracellular sorting and polarized cell surface delivery of (Na+,K+)ATPase, an endogenous component of MDCK cell basolateral plasma membranes. Cell 1986, 46: 623-631. PMID: 3015421, DOI: 10.1016/0092-8674(86)90888-3.Peer-Reviewed Original ResearchConceptsBasolateral plasmalemmal domainsPlasmalemmal domainsNative proteinCell surface deliveryMadin-Darby canine kidney cellsBasolateral plasma membraneBasolateral cell surfacePulse labeling experimentsCanine kidney cellsIntracellular sortingProper sortingSurface deliveryPlasma membraneAcidic compartmentsDarby canine kidney cellsCell surfaceApical surfaceKidney cellsLabeling experimentsTwo-chamber culture systemProteinSortingCulture system