Journal
CURRENT OPINION IN CELL BIOLOGY
Volume 23, Issue 2, Pages 143-149Publisher
CURRENT BIOLOGY LTD
DOI: 10.1016/j.ceb.2010.11.003
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Funding
- Canadian Institutes of Health Research
- National Cancer Institute of Canada
- National Institutes of Health [DP2 OD001925, RO1 DK080955, RO1 CA136577]
- Sandler Program in Basic Sciences
- Burroughs Wellcome Foundation
- Hillbloom Foundation
- Juvenile Diabetes Research Foundation
- Partnership for Cures
- HHMI
- V Foundation
- Steward Trust Foundation
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Inability to meet protein folding demands within the endoplasmic reticulum (ER) activates the unfolded protein response (UPR), a signaling pathway with both adaptive and apoptotic outputs. While some secretory cell types have a remarkable ability to increase protein folding capacity, their upper limits can be reached when pathological conditions overwhelm the fidelity and/or output of the secretory pathway. Irremediable 'ER stress' induces apoptosis and contributes to cell loss in several common human diseases, including type 2 diabetes and neurodegeneration. Researchers have begun to elucidate the molecular switches that determine when ER stress is too great to repair and the signals that are then sent from the UPR to execute the cell.
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