Roles of Endoplasmic Reticulum Stress in Immune Responses
A special issue of Biomedicines (ISSN 2227-9059). This special issue belongs to the section "Immunology and Immunotherapy".
Deadline for manuscript submissions: closed (31 October 2022) | Viewed by 11995
Special Issue Editor
Special Issue Information
Dear Colleagues,
The endoplasmic reticulum (ER) is an important intracellular organelle for protein synthesis, protein folding, protein modification, lipid synthesis, and calcium storage. Impaired ER function causes ER stress due to the accumulation of misfolded or unfolded proteins in the ER lumen. Mammalian cells express three sensor proteins on the ER membrane: IRE1, PERK, and ATF6, which induce three distinct downstream signaling pathways in response to ER stress. These transducers restore ER homeostasis by triggering the unfolded protein response (UPR) that regulates transcriptional and translational programs to reduce ER stress. There has been extensive research in the field of ER stress over the past few decades. Although many studies have reported that ER stress modulates immune responses, the mechanisms by which the UPR signaling pathway regulates ER stress remain unclear. Moreover, research on how ER stress plays a role in the pathogenesis of immune disorders is expected to lead to the development of new immunotherapies targeting the UPR pathway. This Special Issue aims to present aspects of ER stress and the UPR in immune responses, including differentiation, maturation, cell–cell interaction, and cytokine expression in immune cells. We invite authors to submit original research papers and review articles on any aspect of the role of ER stress and UPR signaling in immune responses.
Dr. Jae-Seon So
Guest Editor
Manuscript Submission Information
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Keywords
- ER stress
- unfolded protein response
- IRE1
- PERK
- ATF6
- XBP1s
- ATF4
- immune responses
