2008
Exon Loss Accounts for Differential Sorting of Na-K-Cl Cotransporters in Polarized Epithelial Cells
Carmosino M, Giménez I, Caplan M, Forbush B. Exon Loss Accounts for Differential Sorting of Na-K-Cl Cotransporters in Polarized Epithelial Cells. Molecular Biology Of The Cell 2008, 19: 4341-4351. PMID: 18667527, PMCID: PMC2555935, DOI: 10.1091/mbc.e08-05-0478.Peer-Reviewed Original ResearchConceptsDileucine motifNa-K-Cl cotransporterRenal Na-K-Cl cotransporterPolarized epithelial cellsAmino acid stretchApical proteinsApical sortingEvolutionary lossRenal epithelial cell lineGene structurePhylogenetic analysisDifferential sortingDirect traffickingEpithelial cell lineAdditional exonC-terminusMammalian kidneyApical membraneExonsNovel mechanismNKCC2 geneCell linesBasolateral membraneMotifEpithelial cells
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
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
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 ResearchConceptsApical 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