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Sci. STKE, 11 July 2006
Vol. 2006, Issue 343, p. tw231
[DOI: 10.1126/stke.3432006tw231]

EDITORS' CHOICE

CELL BIOLOGY Fine-Tuning of the Unfolded Protein Response

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 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.

J. Hollien, J. S. Weissman, Decay of endoplasmic reticulum-localized mRNAs during the unfolded protein response. Science 313, 104-107 (2006). [Abstract] [Full Text]

D. Ron, Stressed cells cope with protein overload. Science 313, 52-53 (2006). [Summary] [Full Text]

Citation: Fine-Tuning of the Unfolded Protein Response. Sci. STKE 2006, tw231 (2006).


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