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. 2021 Sep 30;15:685201. doi: 10.3389/fncel.2021.685201

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Copyright © 2021 Shi, Chen, Chen, Yang, Yue, Zhang and Chen.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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The role of sigma-1 receptor in regulating the unfolded protein response signaling. Upon the endoplasmic reticulum (ER) stress, three types of sensors of ER stress: protein kinase RNA-like ER kinase (PERK), inositol-requiring enzyme 1α (IRE1α) and activating transcription factor 6 (ATF6) are evoked and triggers a series of downstream signaling pathways that associated various pathophysiological processes including protein folding, lipid metabolism, energy control, differentiation, inflammation and apoptosis. Upon the ER stress or agonist stimulation, sigma-1 receptor (Sig-1R) dissociates from binding immunoglobulin protein (BiP) and immediately participates in regulating the unfolded protein response (UPR)-dependent signaling pathways.