Please use this identifier to cite or link to this item: http://hdl.handle.net/2445/181312
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dc.contributor.authorJiménez Vidal, Maite-
dc.contributor.authorGasol Escuer, Emma-
dc.contributor.authorZorzano Olarte, Antonio-
dc.contributor.authorNunes Martínez, Virginia-
dc.contributor.authorPalacín Prieto, Manuel-
dc.contributor.authorChillarón Chaves, José Julio-
dc.date.accessioned2021-11-17T14:19:54Z-
dc.date.available2021-11-17T14:19:54Z-
dc.date.issued2004-03-19-
dc.identifier.issn0021-9258-
dc.identifier.urihttp://hdl.handle.net/2445/181312-
dc.description.abstractWe measured sensitivity to thiol modification of the heteromeric glutamate/cystine transporter 4F2hc-xCT expressed in Xenopus oocytes. p-Chloromercuribenzoate (pCMB) and p-chloromercuribenzenesulfonate (pCMBS) rapidly blocked transport activity. Cys(327), located in the middle of the eighth transmembrane domain of the light subunit (xCT), was found to be the main target of inactivation. Cysteine, an impermeant reducing reagent, reversed pCMB and pCMBS effects only when applied from the extracellular medium. l-Glutamate and l-cystine, but not l-arginine, protected from the inactivation with an IC(50) similar to the K(m). Protection was not temperature-dependent, suggesting that it did not depend on large substrate-induced conformational changes. Mutation of Cys(327) to Ala and Ser slightly modified the K(m) and a C327L mutant abolished transport function without compromising transporter expression at the plasma membrane. The results indicate that Cys(327) is a functionally important residue accessible to the aqueous extracellular environment and is structurally linked to the permeation pathway and/or the substrate binding site.-
dc.format.extent8 p.-
dc.format.mimetypeapplication/pdf-
dc.language.isoeng-
dc.publisherAmerican Society for Biochemistry and Molecular Biology-
dc.relation.isformatofReproducció del document publicat a: https://doi.org/10.1074/jbc.M309866200-
dc.relation.ispartofJournal of Biological Chemistry, 2004, vol. 279, num. 12, p. 11214-11221-
dc.relation.urihttps://doi.org/10.1074/jbc.M309866200-
dc.rights(c) American Society for Biochemistry and Molecular Biology, 2004-
dc.sourceArticles publicats en revistes (Ciències Fisiològiques)-
dc.subject.classificationAminoàcids-
dc.subject.classificationProteïnes portadores-
dc.subject.classificationProteïnes de membrana-
dc.subject.otherAmino acids-
dc.subject.otherCarrier proteins-
dc.subject.otherMembrane proteins-
dc.titleThiol modification of cysteine 327 in the eighth transmembrane domain of the light subunit xCT of the heteromeric cystine/glutamate antiporter suggests close proximity to the substrate binding site/permeation pathway-
dc.typeinfo:eu-repo/semantics/article-
dc.typeinfo:eu-repo/semantics/publishedVersion-
dc.identifier.idgrec538532-
dc.date.updated2021-11-17T14:19:54Z-
dc.rights.accessRightsinfo:eu-repo/semantics/openAccess-
dc.identifier.pmid14722095-
Appears in Collections:Articles publicats en revistes (Bioquímica i Biomedicina Molecular)
Articles publicats en revistes (Ciències Fisiològiques)
Articles publicats en revistes (Biologia Cel·lular, Fisiologia i Immunologia)

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