Unfolded Protein Response Signaling and Metabolic Diseases*
- From the Division of Endocrinology, Boston Children's Hospital, Harvard Medical School, Boston, Massachusetts 02115
- ↵1 To whom correspondence should be addressed. E-mail: umut.ozcan{at}childrens.harvard.edu.
Abstract
The endoplasmic reticulum (ER) is a central organelle for protein biosynthesis, folding, and traffic. Perturbations in ER homeostasis create a condition termed ER stress and lead to activation of the complex signaling cascade called the unfolded protein response (UPR). Recent studies have documented that the UPR coordinates multiple signaling pathways and controls various physiologies in cells and the whole organism. Furthermore, unresolved ER stress has been implicated in a variety of metabolic disorders, such as obesity and type 2 diabetes. Therefore, intervening in ER stress and modulating signaling components of the UPR would provide promising therapeutics for the treatment of human metabolic diseases.
Footnotes
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↵* This work was supported, in whole or in part, by National Institutes of Health Grants R01 DK081009 and R01 DK098496 (to U. O.). This work was also supported by American Diabetes Association Career Development Grant 7-09-CD-10 (to U. O.).
- © 2014 by The American Society for Biochemistry and Molecular Biology, Inc.
