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Science 333 (6051): 1830-1831

Copyright © 2011 by the American Association for the Advancement of Science

Sensing ER Stress

Shinichi Kawaguchi1, and Davis T. W. Ng1,2

The endoplasmic reticulum (ER) is sometimes described as the factory of the eukaryotic cell. Most lipids, glycans, and about a third of the proteome are synthesized in this organelle. As with any modern factory, quality control mechanisms are in place to sort and remove defective products from distribution from the ER. A key regulator of this microeconomy is the unfolded protein response (UPR) signaling pathway. On page 1891 in this issue, Gardner and Walter (1) describe a molecular mechanism by which the sensor protein Ire1 detects and communicates ER stress.

1 Temasek Life Sciences Laboratory, National University of Singapore, Singapore 117604.
2 Department of Biological Sciences, National University of Singapore, Singapore 117604.

E-mail: davis{at}tll.org.sg


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Mutual Cross Talk between the Regulators Hac1 of the Unfolded Protein Response and Gcn4 of the General Amino Acid Control of Saccharomyces cerevisiae.
B. Herzog, B. Popova, A. Jakobshagen, H. Shahpasandzadeh, and G. H. Braus (2013)
Eukaryot. Cell 12, 1142-1154
   Abstract »    Full Text »    PDF »
The Unfolded Protein Response: From Stress Pathway to Homeostatic Regulation.
P. Walter and D. Ron (2011)
Science 334, 1081-1086
   Abstract »    Full Text »    PDF »

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