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Oxidative Medicine and Cellular Longevity
Volume 2017, Article ID 2969271, 18 pages
Review Article

Unfolded Protein Response of the Endoplasmic Reticulum in Tumor Progression and Immunogenicity

1Department of Biochemistry, Chungnam National University School of Medicine, Daejeon 35015, Republic of Korea
2Department of Medical Science, Chungnam National University School of Medicine, Daejeon 35015, Republic of Korea

Correspondence should be addressed to Young Joo Jeon;

Received 12 September 2017; Accepted 29 November 2017; Published 21 December 2017

Academic Editor: Dieter Wolf

Copyright © 2017 Yoon Seon Yoo et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


The endoplasmic reticulum (ER) is a pivotal regulator of folding, quality control, trafficking, and targeting of secreted and transmembrane proteins, and accordingly, eukaryotic cells have evolved specialized machinery to ensure that the ER enables these proteins to acquire adequate folding and maturation in the presence of intrinsic and extrinsic insults. This adaptive capacity of the ER to intrinsic and extrinsic perturbations is important for maintaining protein homeostasis, which is termed proteostasis. Failure in adaptation to these perturbations leads to accumulation of misfolded or unassembled proteins in the ER, which is termed ER stress, resulting in the activation of unfolded protein response (UPR) of the ER and the execution of ER-associated degradation (ERAD) to restore homeostasis. Furthermore, both of the two axes play key roles in the control of tumor progression, inflammation, immunity, and aging. Therefore, understanding UPR of the ER and subsequent ERAD will provide new insights into the pathogenesis of many human diseases and contribute to therapeutic intervention in these diseases.