File Download

There are no files associated with this item.

  Links for fulltext
     (May Require Subscription)
Supplementary

Article: Disulphide production by Ero1α-PDI relay is rapid and effectively regulated

TitleDisulphide production by Ero1α-PDI relay is rapid and effectively regulated
Authors
Keywordsendoplasmic reticulum
disulphide-bond formation
Ero1
glutathione
protein disulphide isomerase
Issue Date2010
Citation
EMBO Journal, 2010, v. 29, n. 19, p. 3318-3329 How to Cite?
AbstractThe molecular networks that control endoplasmic reticulum (ER) redox conditions in mammalian cells are incompletely understood. Here, we show that after reductive challenge the ER steady-state disulphide content is restored on a time scale of seconds. Both the oxidase Ero1α and the oxidoreductase protein disulphide isomerase (PDI) strongly contribute to the rapid recovery kinetics, but experiments in ERO1-deficient cells indicate the existence of parallel pathways for disulphide generation. We find PDI to be the main substrate of Ero1α, and mixed-disulphide complexes of Ero1 primarily form with PDI, to a lesser extent with the PDI-family members ERp57 and ERp72, but are not detectable with another homologue TMX3. We also show for the first time that the oxidation level of PDIs and glutathione is precisely regulated. Apparently, this is achieved neither through ER import of thiols nor by transport of disulphides to the Golgi apparatus. Instead, our data suggest that a dynamic equilibrium between Ero1-and glutathione disulphide-mediated oxidation of PDIs constitutes an important element of ER redox homeostasis. © 2010 European Molecular Biology Organization | All Rights Reserved.
Persistent Identifierhttp://hdl.handle.net/10722/205737
ISSN
2015 Impact Factor: 9.643
2015 SCImago Journal Rankings: 7.450
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorAppenzeller-Herzog, Christian-
dc.contributor.authorRiemer, Jan-
dc.contributor.authorZito, Ester-
dc.contributor.authorChin, Kingtung-
dc.contributor.authorRon, David-
dc.contributor.authorSpiess, Martin-
dc.contributor.authorEllgaard, Lars-
dc.date.accessioned2014-10-06T08:02:17Z-
dc.date.available2014-10-06T08:02:17Z-
dc.date.issued2010-
dc.identifier.citationEMBO Journal, 2010, v. 29, n. 19, p. 3318-3329-
dc.identifier.issn0261-4189-
dc.identifier.urihttp://hdl.handle.net/10722/205737-
dc.description.abstractThe molecular networks that control endoplasmic reticulum (ER) redox conditions in mammalian cells are incompletely understood. Here, we show that after reductive challenge the ER steady-state disulphide content is restored on a time scale of seconds. Both the oxidase Ero1α and the oxidoreductase protein disulphide isomerase (PDI) strongly contribute to the rapid recovery kinetics, but experiments in ERO1-deficient cells indicate the existence of parallel pathways for disulphide generation. We find PDI to be the main substrate of Ero1α, and mixed-disulphide complexes of Ero1 primarily form with PDI, to a lesser extent with the PDI-family members ERp57 and ERp72, but are not detectable with another homologue TMX3. We also show for the first time that the oxidation level of PDIs and glutathione is precisely regulated. Apparently, this is achieved neither through ER import of thiols nor by transport of disulphides to the Golgi apparatus. Instead, our data suggest that a dynamic equilibrium between Ero1-and glutathione disulphide-mediated oxidation of PDIs constitutes an important element of ER redox homeostasis. © 2010 European Molecular Biology Organization | All Rights Reserved.-
dc.languageeng-
dc.relation.ispartofEMBO Journal-
dc.subjectendoplasmic reticulum-
dc.subjectdisulphide-bond formation-
dc.subjectEro1-
dc.subjectglutathione-
dc.subjectprotein disulphide isomerase-
dc.titleDisulphide production by Ero1α-PDI relay is rapid and effectively regulated-
dc.typeArticle-
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1038/emboj.2010.203-
dc.identifier.pmid20802462-
dc.identifier.scopuseid_2-s2.0-77957806157-
dc.identifier.volume29-
dc.identifier.issue19-
dc.identifier.spage3318-
dc.identifier.epage3329-
dc.identifier.eissn1460-2075-
dc.identifier.isiWOS:000283700700010-

Export via OAI-PMH Interface in XML Formats


OR


Export to Other Non-XML Formats