Journal
TRENDS IN ENDOCRINOLOGY AND METABOLISM
Volume 27, Issue 10, Pages 731-741Publisher
ELSEVIER SCIENCE LONDON
DOI: 10.1016/j.tem.2016.06.002
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Funding
- Department of Defense Breast Cancer Research Program [W81 XWH-14-1-0159]
- National Institute of Diabetes and Digestive and Kidney Diseases of the National Institutes of Health [RO1 DK071909]
- National Science Foundation [DGE-114245]
- University of Illinois, Department of Biochemistry
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The endoplasmic reticulum (EnR) stress sensor, the unfolded protein response (UPR), plays a key role in regulating intracellular protein homeostasis. The extensively studied reactive mode of UPR activation is characterized by unfolded protein, or other EnR stress, triggering UPR activation. Here we focus on the emerging anticipatory mode of UPR activation in which mitogenic steroid and peptide hormones and other effectors preactivate the UPR and anticipate a future need for increased protein folding capacity. Mild UPR activation in breast cancer can be protective and contributes to antiestrogen resistance. Hyper activation of the anticipatory UPR pathway in cancer cells with a small molecule converts it from cytoprotective to cytotoxic, highlighting its potential as a therapeutic target in estrogen receptor-positive breast cancer.
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