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
2007
MAL decreases the internalization of the aquaporin-2 water channel
Kamsteeg EJ, Duffield AS, Konings IB, Spencer J, Pagel P, Deen PM, Caplan MJ. MAL decreases the internalization of the aquaporin-2 water channel. Proceedings Of The National Academy Of Sciences Of The United States Of America 2007, 104: 16696-16701. PMID: 17940053, PMCID: PMC2034241, DOI: 10.1073/pnas.0708023104.Peer-Reviewed Original ResearchConceptsAquaporin-2 water channelIntracellular vesiclesApical membrane proteinsMembrane-associated proteinsTrafficking of AQP2Apical surface expressionEpithelial cellsCell surface retentionApical plasma membraneInvolvement of MALBody water homeostasisS256 phosphorylationWater channel proteinsSurface expressionApical deliveryRegulated traffickingSorting eventsRenal epithelial cellsMembrane associationMembrane proteinsPosttranslational modificationsProtein interactionsPlasma membraneChannel proteinsWater channelsTransport 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 ResearchMeSH KeywordsAnimalsCell PolarityEpithelial CellsHumansMembrane Transport ProteinsProtein TransportSignal TransductionConceptsTransport 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
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 ResearchMeSH KeywordsAmino Acid MotifsAnimalsCell LineDogsHomeostasisIntracellular MembranesMembrane Transport ProteinsSignal TransductionConceptsBasolateral 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
2001
The NH2-terminus of Norepinephrine Transporter Contains a Basolateral Localization Signal for Epithelial Cells
Gu H, Wu X, Giros B, Caron M, Caplan M, Rudnick G. The NH2-terminus of Norepinephrine Transporter Contains a Basolateral Localization Signal for Epithelial Cells. Molecular Biology Of The Cell 2001, 12: 3797-3807. PMID: 11739781, PMCID: PMC60756, DOI: 10.1091/mbc.12.12.3797.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsCell LineCell PolarityDogsDopamine Plasma Membrane Transport ProteinsEpithelial CellsHumansMembrane GlycoproteinsMembrane Transport ProteinsMiceMicroscopy, ConfocalMolecular Sequence DataMutagenesis, Site-DirectedNerve Tissue ProteinsNorepinephrine Plasma Membrane Transport ProteinsProtein Sorting SignalsSequence AlignmentSymportersConceptsBasolateral localization signalLocalization signalDileucine motifPlasma membraneBasolateral localizationOverall amino acid sequence identityAmino acid sequence identityTerminal regionMDCK cellsApical plasma membraneBasolateral membraneEpithelial cellsSequence identityApical localizationChimeric proteinTransport assaysTransporter localizationAmino acidsApical membraneNorepinephrine transporterTransportersCorresponding sequenceDopamine transporterSame mutationMembrane
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[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
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
SORTING OF GABA TRANSPORTER PROTEINS IN POLARIZED CELLS
CAPLAN M. SORTING OF GABA TRANSPORTER PROTEINS IN POLARIZED CELLS. Neurochemistry International 1996, 29: 357-360. PMID: 8939443, DOI: 10.1016/0197-0186(95)00159-x.Peer-Reviewed Original ResearchCell-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 transporterPolarized 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
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