New insights into oxidative folding

The oxidoreductase ERO1 (endoplasmic reticulum [ER] oxidoreductin 1) is thought to be crucial for disulfide bond formation in the ER. In this issue, Zito et al. (2010. J. Cell Biol. doi:10.1083/jcb.200911086) examine the division of labor between the two mammalian isoforms of ERO1 (ERO1-α and -β) in...

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Detalles Bibliográficos
Autor principal: Sevier, Carolyn S.
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 2010
Materias:
Reviews
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2845070/
https://www.ncbi.nlm.nih.gov/pubmed/20308423
http://dx.doi.org/10.1083/jcb.201002114
Descripción
Sumario:The oxidoreductase ERO1 (endoplasmic reticulum [ER] oxidoreductin 1) is thought to be crucial for disulfide bond formation in the ER. In this issue, Zito et al. (2010. J. Cell Biol. doi:10.1083/jcb.200911086) examine the division of labor between the two mammalian isoforms of ERO1 (ERO1-α and -β) in oxidative folding. Their analysis reveals a selective role for ERO1-β in insulin production and a surprisingly minor contribution for either ERO1 isoform on immunoglobulin folding and secretion.

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