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Science 318 (5852): 944-949

Copyright © 2007 by the American Association for the Advancement of Science

IRE1 Signaling Affects Cell Fate During the Unfolded Protein Response

Jonathan H. Lin,1,2,3* Han Li,1,2 Douglas Yasumura,4 Hannah R. Cohen,2 Chao Zhang,1,5 Barbara Panning,2 Kevan M. Shokat,1,5 Matthew M. LaVail,4 Peter Walter1,2

Abstract: Endoplasmic reticulum (ER) stress activates a set of signaling pathways, collectively termed the unfolded protein response (UPR). The three UPR branches (IRE1, PERK, and ATF6) promote cell survival by reducing misfolded protein levels. UPR signaling also promotes apoptotic cell death if ER stress is not alleviated. How the UPR integrates its cytoprotective and proapoptotic outputs to select between life or death cell fates is unknown. We found that IRE1 and ATF6 activities were attenuated by persistent ER stress in human cells. By contrast, PERK signaling, including translational inhibition and proapoptotic transcription regulator Chop induction, was maintained. When IRE1 activity was sustained artificially, cell survival was enhanced, suggesting a causal link between the duration of UPR branch signaling and life or death cell fate after ER stress. Key findings from our studies in cell culture were recapitulated in photoreceptors expressing mutant rhodopsin in animal models of retinitis pigmentosa.

1 Howard Hughes Medical Institute, University of California at San Francisco, San Francisco, CA 94158, USA.
2 Department of Biochemistry and Biophysics, University of California at San Francisco, San Francisco, CA 94158, USA.
3 Departments of Pathology and Ophthalmology, University of California at San Francisco, San Francisco, CA 94158, USA.
4 Departments of Anatomy and Ophthalmology, University of California at San Francisco, San Francisco, CA 94158, USA.
5 Department of Cellular and Molecular Pharmacology, University of California at San Francisco, San Francisco, CA 94158, USA.

* To whom correspondence should be addressed. E-mail: Jonathan.Lin{at}ucsf.edu


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F. Torres-Quiroz, S. Garcia-Marques, R. Coria, F. Randez-Gil, and J. A. Prieto (2010)
J. Biol. Chem. 285, 20088-20096
   Abstract »    Full Text »    PDF »
Late Phase of the Endoplasmic Reticulum Stress Response Pathway Is Regulated by Hog1 MAP Kinase.
A. A. Bicknell, J. Tourtellotte, and M. Niwa (2010)
J. Biol. Chem. 285, 17545-17555
   Abstract »    Full Text »    PDF »
ER stress and the unfolded protein response in intestinal inflammation.
M. A. McGuckin, R. D. Eri, I. Das, R. Lourie, and T. H. Florin (2010)
Am J Physiol Gastrointest Liver Physiol 298, G820-G832
   Abstract »    Full Text »    PDF »
Regulation of basal cellular physiology by the homeostatic unfolded protein response.
D. T. Rutkowski and R. S. Hegde (2010)
J. Cell Biol. 189, 783-794
   Abstract »    Full Text »    PDF »
Activity-Dependent Augmentation of Spontaneous Neurotransmission during Endoplasmic Reticulum Stress.
E. Nosyreva and E. T. Kavalali (2010)
J. Neurosci. 30, 7358-7368
   Abstract »    Full Text »    PDF »
AlphaScreen(R)-Based Characterization of the Bifunctional Kinase/RNase IRE1{alpha}: A Novel and Atypical Drug Target.
M. Bouchecareilh, M. E. Caruso, P. Roby, S. Parent, N. Rouleau, S. Taouji, O. Pluquet, R. Bosse, M. Moenner, and E. Chevet (2010)
J Biomol Screen 15, 406-417
   Abstract »    Full Text »    PDF »
Treatment with Panobinostat Induces Glucose-Regulated Protein 78 Acetylation and Endoplasmic Reticulum Stress in Breast Cancer Cells.
R. Rao, S. Nalluri, R. Kolhe, Y. Yang, W. Fiskus, J. Chen, K. Ha, K. M. Buckley, R. Balusu, V. Coothankandaswamy, et al. (2010)
Mol. Cancer Ther. 9, 942-952
   Abstract »    Full Text »    PDF »
Restoration of visual function in P23H rhodopsin transgenic rats by gene delivery of BiP/Grp78.
M. S. Gorbatyuk, T. Knox, M. M. LaVail, O. S. Gorbatyuk, S. M. Noorwez, W. W. Hauswirth, J. H. Lin, N. Muzyczka, and A. S. Lewin (2010)
PNAS 107, 5961-5966
   Abstract »    Full Text »    PDF »
Chimeric tRNAs as tools to induce proteome damage and identify components of stress responses.
R. Geslain, L. Cubells, T. Bori-Sanz, R. Alvarez-Medina, D. Rossell, E. Marti, and L. R. de Pouplana (2010)
Nucleic Acids Res. 38, e30
   Abstract »    Full Text »    PDF »
Alisol B, a Novel Inhibitor of the Sarcoplasmic/Endoplasmic Reticulum Ca2+ ATPase Pump, Induces Autophagy, Endoplasmic Reticulum Stress, and Apoptosis.
B. Y. K. Law, M. Wang, D.-L. Ma, F. Al-Mousa, F. Michelangeli, S.-H. Cheng, M. H. L. Ng, K.-F. To, A. Y. F. Mok, R. Y. Y. Ko, et al. (2010)
Mol. Cancer Ther. 9, 718-730
   Abstract »    Full Text »    PDF »
Regulation of Endoplasmic Reticulum Stress-induced Cell Death by ATF4 in Neuroectodermal Tumor Cells.
J. L. Armstrong, R. Flockhart, G. J. Veal, P. E. Lovat, and C. P. F. Redfern (2010)
J. Biol. Chem. 285, 6091-6100
   Abstract »    Full Text »    PDF »

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