The role of the unfolded protein response in tumour development: friend or foe?

By Yanjun Ma, L. Hendershot. Nature Reviews. Cancer, 2004

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ER stress‐regulated translation increases tolerance to extreme hypoxia and promotes tumor growth (2005, background): “Prolonged hypoxia induces apoptosis in a PERK-dependent manner Cells with a compromised UPR are more susceptible to ER stress-induced apoptosis compared to cells with an intact UPR (Kaufman, 2002; Ma and Hendershot, 2004).”
The unfolded protein response signals through high-order assembly of Ire1 (2008, neutral): “TheUPRisactivatedincancers 3,4 , viral infections 5 , protein-folding diseases 6,7 and other cellular anomalies 8,9 .”
The Role of the PERK/eIF2α/ATF4/CHOP Signaling Pathway in Tumor Progression During Endoplasmic Reticulum Stress (2016, background): “These disruptions rapidly lead to the aggregation of unfolded and misfolded proteins in the lumen of the ER, further activating the UPR signaling branches as a cellular adaptive program to cope with stress conditions, recover the homeostatic state, and resume cell division [9, 19, 20].”
GRP78 induction in cancer: therapeutic and prognostic implications. (2007, background): “When the protein load exceeds the folding capacity of the ER, the cells trigger the unfolded protein response (UPR), which activates the PERK, IRE1/X-box binding protein-1 (XBP-1), and activating transcription factor-6 (ATF6) signaling pathways as protective measures, resulting in general translatio”