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
A Transmembrane Segment Determines the Steady-State Localization of an Ion-Transporting Adenosine Triphosphatase
Dunbar L, Aronson P, Caplan M. A Transmembrane Segment Determines the Steady-State Localization of an Ion-Transporting Adenosine Triphosphatase. Journal Of Cell Biology 2000, 148: 769-778. PMID: 10684257, PMCID: PMC2169368, DOI: 10.1083/jcb.148.4.769.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBiological TransportCationsCell LineCell MembraneCell PolarityGlycosphingolipidsGlycosylphosphatidylinositolsH(+)-K(+)-Exchanging ATPaseHydrogen-Ion ConcentrationMembrane ProteinsMolecular Sequence DataOuabainParietal Cells, GastricProtein Sorting SignalsRecombinant Fusion ProteinsSequence AlignmentSequence DeletionSodium-Potassium-Exchanging ATPaseSolubilityTransfectionConceptsK-ATPase alpha subunitAlpha subunitTransmembrane domainPolytopic membrane transport proteinK-ATPaseApical distributionGlycosphingolipid-rich membrane domainsDetergent-insoluble complexesMembrane transport proteinsApical membrane proteinsApical plasma membraneK-ATPase alphaFourth transmembrane domainLocalization signalChimeric pumpsFourth transmembraneTransmembrane segmentsK-ATPase sequencesMembrane compartmentsMembrane domainsMembrane proteinsSequence domainsPlasma membraneGastric parietal cellsTransport proteins
1993
An ion-transporting ATPase encodes multiple apical localization signals.
Gottardi CJ, Caplan MJ. An ion-transporting ATPase encodes multiple apical localization signals. Journal Of Cell Biology 1993, 121: 283-293. PMID: 8385670, PMCID: PMC2200096, DOI: 10.1083/jcb.121.2.283.Peer-Reviewed Original ResearchConceptsK-ATPaseIon-transporting ATPaseDifferential subcellular distributionEpithelial cell typesEpithelial sortingEpithelial cellsEndocytosis signalLocalization signalEndocytic pathwayMembrane proteinsPlasmalemmal domainsApical localizationMolecular signalsSubcellular distributionBeta subunitRenal proximal tubular epithelial cellsCell typesIon pumpsApical surfaceDistinct populationsFull lengthBasolateral membraneProximal tubular epithelial cellsIndependent signalsTubular epithelial cells