Crosstalk with Unfolded Protein Response (UPR) Signaling Networks

A special issue of Genes (ISSN 2073-4425). This special issue belongs to the section "Epigenomics".

Deadline for manuscript submissions: closed (10 November 2022) | Viewed by 2183

Special Issue Editor


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Guest Editor
Department of Biological Sciences, University of Wisconsin, Milwaukee, WI 53201, USA
Interests: endoplasmic reticulum

Special Issue Information

Dear Colleagues,

Accumulation of misfolded or unfolded protein inside the endoplasmic reticulum activates the unfolded protein response (UPR) pathways. The UPR promotes cell survival by restoring ER protein homeostasis (adaptive response), but if it fails, the UPR induces cell death (apoptotic response). According to the current model, three ER-transmembrane proteins (IRE1, PERK, and ATF6) sense and signal the UPR. The recent biological information from genome, proteome, and related projects indicates that components of several intracellular signaling pathways act as effectors and modulators of the UPR pathways. Therefore, the UPR should not be viewed as three independent signaling pathways, but instead as a network of integrated signaling pathways. In this Special Issue, we seek to publish a collection of original research articles, mini reviews, and commentaries related to the crosstalk and coregulation of the UPR pathways to synergistically modulate the adaptive and/or apoptotic responses.

Prof. Dr. Madhusudan Dey
Guest Editor

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Published Papers (1 paper)

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Research

11 pages, 1783 KiB  
Article
Prx1 Regulates Thapsigargin-Mediated UPR Activation and Apoptosis
by Eun-Kyung Kim, Yosup Kim, Jun Young Yang and Ho Hee Jang
Genes 2022, 13(11), 2033; https://doi.org/10.3390/genes13112033 - 4 Nov 2022
Cited by 4 | Viewed by 1828
Abstract
Endoplasmic reticulum (ER) stress activates the unfolded protein response (UPR) signaling via the accumulation of unfolded and misfolded proteins. ER stress leads to the production of reactive oxygen species (ROS), which are necessary to maintain redox homeostasis in the ER. Although peroxiredoxin 1 [...] Read more.
Endoplasmic reticulum (ER) stress activates the unfolded protein response (UPR) signaling via the accumulation of unfolded and misfolded proteins. ER stress leads to the production of reactive oxygen species (ROS), which are necessary to maintain redox homeostasis in the ER. Although peroxiredoxin 1 (Prx1) is an antioxidant enzyme that regulates intracellular ROS levels, the link between Prx1 and ER stress remains unclear. In this study, we investigated the role of Prx1 in X-box binding protein 1 (XBP-1) activation, the C/EBP homologous protein (CHOP) pathway, and apoptosis in response to ER stress. We observed that Prx1 overexpression inhibited the nuclear localization of XBP-1 and the expression of XBP-1 target genes and CHOP after thapsigargin (Tg) treatment to induce ER stress. In addition, Prx1 inhibited apoptosis and ROS production during ER stress. The ROS scavenger inhibited ER stress-induced apoptosis but did not affect XBP-1 activation and CHOP expression. Therefore, the biological role of Prx1 in ER stress may have important implications for ER stress-related diseases. Full article
(This article belongs to the Special Issue Crosstalk with Unfolded Protein Response (UPR) Signaling Networks)
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