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
1998
Conformational alterations resulting from mutations in cytoplasmic domains of the alpha subunit of the Na,K-ATPase.
Blostein R, Daly SE, Boxenbaum N, Lane LK, Arguello JM, Lingrel JB, Karlish SJ, Caplan MJ, Dunbar L. Conformational alterations resulting from mutations in cytoplasmic domains of the alpha subunit of the Na,K-ATPase. Acta Physiologica Scandinavica. Supplementum 1998, 643: 275-81. PMID: 9789570.Peer-Reviewed Original ResearchConceptsM2-M3 loopCytoplasmic domainCytoplasmic loopK-ATPaseN-terminusStructure/function analysisTransmembrane segment M2Amino-terminal halfMajor cytoplasmic loopFifth transmembrane segmentFirst cytoplasmic loopCatalytic phosphorylation siteMajor conformational statesLow catalytic turnoverPutative cationCytoplasmic mutantsTransmembrane segmentsPhosphorylation sitesTransmembrane domainAlpha 1 subunitSegment M2Cytoplasmic regionApparent affinityAmino terminusTerminal halfSorting of P-type ATPases in polarized epithelial cells.
Dunbar LA, Courtois-Coutry N, Roush DL, Muth TR, Gottardi CJ, Rajendran V, Geibel J, Kashgarian M, Caplan MJ. Sorting of P-type ATPases in polarized epithelial cells. Acta Physiologica Scandinavica. Supplementum 1998, 643: 289-95. PMID: 9789572.Peer-Reviewed Original ResearchConceptsApical localizationK-ATPaseMost epithelial cell typesTyrosine-based signalsP-type familyP-type ATPasesEpithelial cellsCritical tyrosine residuesApical plasma membraneFourth transmembrane domainBeta-subunit sequencesApical cell surfaceEpithelial cell typesSorting signalsTransmembrane domainCytoplasmic tailSequence domainsPlasma membraneHomologous membersTyrosine residuesParietal cellsStorage compartmentCell typesCell surfaceBasolateral surface