Dimerization of ER-resident molecular chaperones mediated by ERp29
- PMID: 33360823
- DOI: 10.1016/j.bbrc.2020.12.023
Dimerization of ER-resident molecular chaperones mediated by ERp29
Abstract
The lectin chaperones calnexin (CNX) and calreticulin (CRT) localized in the endoplasmic reticulum play important roles in glycoprotein quality control. Although the interaction between these lectin chaperones and ERp57 is well known, it has been recently reported that endoplasmic reticulum protein 29 (ERp29), a member of PDI family, interacts with CNX and CRT. The biochemical function of ERp29 is unclear because it exhibits no ERp57-like redox activity. In this study, we addressed the possibility that ER chaperones CNX and CRT are connected via ERp29, based on our observation that ERp29 exists as a dimer. As a result, we showed that CNX dimerizes through ERp29. These results endorse the hypothesis that ERp29 serves as a bridge that links two molecules of CNX. Also, we showed that similar complexes such as CNX-CRT were formed via ERp29.
Keywords: Calnexin; Calreticulin; Endoplasmic reticulum; Endoplasmic reticulum protein 29; Molecular chaperone.
Copyright © 2020 Elsevier Inc. All rights reserved.
Conflict of interest statement
Declaration of competing interest The authors have no conflicts of interest to declare.
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