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. 2019 Oct 31;20(6):4774–4780. doi: 10.3892/mmr.2019.10789

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Copyright: © Mao et al.

This is an open access article distributed under the terms of the Creative Commons Attribution-NonCommercial-NoDerivs License, which permits use and distribution in any medium, provided the original work is properly cited, the use is non-commercial and no modifications or adaptations are made.

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Figure 1. — A variety of physiological conditions can disrupt the protein folding process and consequently result in the accumulation of unfolded and misfolded proteins in the ER, a condition termed ER stress. Under ER stress, the UPR is activated to minimize overloading. If the UPR is successful in reducing the number of unfolded and misfolded proteins, UPR signaling is attenuated and the cell survives. ER, endoplasmic reticulum; GRP78, 78-kDa glucose-regulated protein; PERK, protein kinase R-like ER kinase; eIF2α, eukaryotic translation initiation factor 2α; ATF4, activating transcription factor 4; ATF6, activating transcription factor 6; IRE1α, inositol-requiring enzyme 1α; XBP1, X-box binding protein 1; ERAD, endoplasmic reticulum associated degradation; UPR, unfolded protein response.