We use cookies to ensure that we give you the best experience on our website. You can change your cookie settings at any time. Otherwise, we'll assume you're OK to continue.

Durham University

Department of Chemistry

Publication details for Prof. Ritu Kataky

Dias-Gunasekara, S., van Lith, M., Kataky, R., Williams, G. & Benham, A.M. (2006). Expression, interactions and dynamics of the oxidoreductase Ero1Lbeta. FASEB journal 20(4): A500.

Author(s) from Durham


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.