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Expression, interactions and dynamics of the oxidoreductase Ero1Lbeta

Dias-Gunasekara, S.; van Lith, M.; Kataky, R.; Williams, G.; Benham, A.M.


S. Dias-Gunasekara

M. van Lith

G. Williams

A.M. Benham


Protein oxidation in the Endoplasmic Reticulum (ER) is catalysed by Endoplasmic reticulum oxidoreductases (EROs) that donate disulfide bonds to (and accept electrons from) Protein Disulfide Isomerase (PDI). Eros are essential for viability and protein secretion in yeast. Objective: we have studied the mammalian Ero1p homolog, Ero1beta to in order to understand the expression, interaction partners and ultimately function of EROs in multicellular organisms. Methods: We have used immunohistochemistry to examine the localization of Ero1beta and other ER chaperones in mouse and human tissues. Western blotting, pulse chase analysis and co-immunoprecipitation was used in combination with non-reducing SDS-PAGE to determine the oxidation status, half life and disulfide-dependent complex formation of Ero1beta and its partners. Conclusion: We find that Ero1beta is highly expressed in certain secretory tissues such as stomach and pancreas. Ero1beta is not expressed in most cell lines in the absence of an unfolded protein response. Like Ero1alpha, Ero1beta interacts with PDI and can also form disulfide dependent dimers that depend on the CXXCXXC active site. These dimers may have a role in regulating disulfide bond formation.


Dias-Gunasekara, S., van Lith, M., Kataky, R., Williams, G., & Benham, A. (2006). Expression, interactions and dynamics of the oxidoreductase Ero1Lbeta. FASEB Journal, 20(4),

Journal Article Type Article
Online Publication Date Mar 6, 2006
Publication Date 2006-03
Journal FASEB Journal
Print ISSN 0892-6638
Electronic ISSN 1530-6860
Publisher Federation of American Society of Experimental Biology (FASEB)
Peer Reviewed Peer Reviewed
Volume 20
Issue 4
Public URL
Publisher URL