Fine-Tuning of the Unfolded Protein Response

Science  07 Jul 2006:
Vol. 313, Issue 5783, pp. 13k
DOI: 10.1126/science.313.5783.13k

The unfolded protein response (UPR) plays a central role in governing a cell's survival after exposure to stress. The UPR encompasses a diverse range of transcriptional and translational responses stimulated by the increase in levels of unfolded or misfolded proteins within the endoplasmic reticulum (ER). The UPR uses different strategies to provide a coherent response, which allows cells both to survive acute folding stresses and to fine-tune the ER folding capacity to meet the needs of a cell. Hollien and Weissman (p. 104; see the Perspective by Ron) systematically explored the outputs of various players in the UPR. They found that IRE1 (the transmembrane protein that monitors the folding status of the ER) mediates a rapid and robust down-regulation of a subset of ER-targeted messages by direct destabilization of ER-bound messenger RNAs.

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