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The mammalian unfolded protein response

Schröder, M.; Kaufman, R.J.

Authors

R.J. Kaufman



Abstract

In the endoplasmic reticulum (ER) secretory and transmembrane proteins fold into their native conformation and undergo posttranslational modifications important for their activity and structure. When protein folding in the ER is inhibited, signal transduction pathways, which increase the biosynthetic capacity and decrease the biosynthetic burden of the ER to maintain the homeostasis of this organelle, are activated. These pathways are called the unfolded protein response (UPR). In this review, we briefly summarize principles of protein folding and molecular chaperone function important for a mechanistic understanding of UPR-signaling events. We then discuss mechanisms of signal transduction employed by the UPR in mammals and our current understanding of the remodeling of cellular processes by the UPR. Finally, we summarize data that demonstrate that UPR signaling feeds into decision making in other processes previously thought to be unrelated to ER function, e.g., eukaryotic starvation responses and differentiation programs.

Citation

Schröder, M., & Kaufman, R. (2005). The mammalian unfolded protein response. Annual Review of Biochemistry, 74, 739-789

Journal Article Type Article
Publication Date 2005
Journal Annual Review of Biochemistry
Print ISSN 0066-4154
Electronic ISSN 1545-4509
Publisher Annual Reviews
Peer Reviewed Peer Reviewed
Volume 74
Pages 739-789
Keywords Unfolded protein response; endoplasmic reticulum; chaperone; calnexin
Public URL https://durham-repository.worktribe.com/output/1572838
Publisher URL http://arjournals.annualreviews.org/doi/abs/10.1146/annurev.biochem.73.011303.074134