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Szegezdi, E,Logue, SE,Gorman, AM,Samali, A
2006
September
Mediators of endoplasmic reticulum stress-induced apoptosis
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1
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apoptosis BCL2 family ER stress unfolded protein response UNFOLDED PROTEIN RESPONSE INDUCED CELL-DEATH ER-STRESS INDUCIBLE PROTEIN PROAPOPTOTIC BAX ACTIVATION CASPASE-12 IRE1 P58(IPK) BCL-2
The efficient functioning of the endoplasmic reticulum ( ER) is essential for most cellular activities and survival. Conditions that interfere with ER function lead to the accumulation and aggregation of unfolded proteins. ER transmembrane receptors detect the onset of ER stress and initiate the unfolded protein response ( UPR) to restore normal ER function. If the stress is prolonged, or the adaptive response fails, apoptotic cell death ensues. Many studies have focused on how this failure initiates apoptosis, as ER stress- induced apoptosis is implicated in the pathophysiology of several neurodegenerative and cardiovascular diseases. In this review, we examine the role of the molecules that are activated during the UPR in order to identify the molecular switch from the adaptive phase to apoptosis. We discuss how the activation of these molecules leads to the commitment of death and the mechanisms that are responsible for the final demise of the cell.
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DOI 10.1038/sj.embor.7400779
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