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FEBS J. 2017 Dec 14. doi: 10.1111/febs.14359. [Epub ahead of print]

Regulation of tumor-stroma interactions by the unfolded protein response.

Author information

1
Inserm U1242 'Chemistry, Oncogenesis, Stress & Signaling', Université de Rennes, Rennes, France.
2
Centre de Lutte Contre le Cancer Eugene Marquis, Rennes, France.
3
INSERM, C3M, Université Côte d'Azur, Nice, France.
4
Department of Medicine, University of California, San Francisco, San Francisco, CA, USA.

Abstract

The unfolded protein response (UPR) is a conserved adaptive pathway that helps cells cope with the protein misfolding burden within the endoplasmic reticulum (ER). Imbalance between protein folding demand and capacity in the ER leads to a situation called ER stress that is often observed in highly proliferative and secretory tumor cells. As such, activation of the UPR signaling has emerged as a key adaptive mechanism promoting cancer progression. It is becoming widely acknowledged that, in addition to its intrinsic effect on tumor biology, the UPR can also regulate tumor microenvironment. In this review, we discuss how the UPR coordinates the crosstalk between tumor and stromal cells, such as endothelial cells, normal parenchymal cells, and immune cells. In addition, we further describe the involvement of ER stress signaling in the response to current treatments as well as its impact on antitumor immunity mainly driven by immunogenic cell death. Finally, in this context, we discuss the relevance of targeting ER stress/UPR signaling as a potential anticancer approach.

KEYWORDS:

ER stress; immunogenic cell death; inflammation; tumor microenvironment; unfolded protein response

PMID:
29239107
DOI:
10.1111/febs.14359
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