ArticleiScience2026
Regulation of the endoplasmic reticulum stress sensor ATF6α through multiple oxidoreductases in the ER.
Article in iScience, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
1 citing paper in PubMed.
- Targeting Insulin Signaling and TRAF2/JNK Pathway: A Comprehensive In Silico Study ofInternational journal of molecular sciences · 2026Article
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The unfolded protein response (UPR) maintains cellular homeostasis during ER stress. In this process, activating transcription factor 6α (ATF6α) is activated through several multi-step processes, including transport to the Golgi apparatus, and plays an important role as a UPR sensor. Disulfide bond-mediated dimerization of ATF6α contributes to efficient transport to the Golgi apparatus. However, this regulatory mechanism remains unclear. Here, we show that ER-resident oxidoreductases, including ERdj5 and PDIR, promote C467 dimerization, whereas ERp18 inhibits this process. In particular, ERdj5 facilitates C467 dimerization via Trx2 and reduces C618 dimerization via Trx3, supporting ATF6α activation. Furthermore, ATF6α dimerization stabilizes its structure and prevents its degradation by ER-associated degradation (ERAD). Our findings reveal that multiple oxidoreductases participate in the regulation of ATF6α activation during ER stress.
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