title: Signaling cell death from the endoplasmic reticulum stress response.
abstract: 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.
authors.affiliation: Department of Biochemistry and Goodman Cancer Center, McGill University, Montreal, Quebec, H3G 1Y6, Canada. gordon.shore@mcgill.ca
authors.forename: Gordon C
authors.initials: GC
authors.lastname: Shore
authors.forename: Feroz R
authors.initials: FR
authors.lastname: Papa
authors.forename: Scott A
authors.initials: SA
authors.lastname: Oakes
mesh_terms: D000818:Animals; D016923:Cell Death; D004721:Endoplasmic Reticulum / Q000378:metabolism*; D006801:Humans; D058767:Protein Unfolding; D015398:Signal Transduction; D013312:Stress, Physiological