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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 signalingpathways, collectively termed the unfolded protein response(UPR). The three UPR branches (IRE1, PERK, and ATF6) promotecell survival by reducing misfolded protein levels. UPR signalingalso promotes apoptotic cell death if ER stress is not alleviated.How the UPR integrates its cytoprotective and proapoptotic outputsto select between life or death cell fates is unknown. We foundthat IRE1 and ATF6 activities were attenuated by persistentER stress in human cells. By contrast, PERK signaling, includingtranslational inhibition and proapoptotic transcription regulatorChop induction, was maintained. When IRE1 activity was sustainedartificially, cell survival was enhanced, suggesting a causallink between the duration of UPR branch signaling and life ordeath cell fate after ER stress. Key findings from our studiesin cell culture were recapitulated in photoreceptors expressingmutant 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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[DOI: 10.1126/stke.4122007tw412] |Abstract »
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186, 323-331
|Abstract »|Full Text »|PDF »
Induction of endoplasmic reticulum stress response by TZD18, a novel dual ligand for peroxisome proliferator-activated receptor {alpha}/{gamma}, in human breast cancer cells.
C. Zang, H. Liu, J. Bertz, K. Possinger, H. P. Koeffler, E. Elstner, and J. Eucker (2009)
Mol. Cancer Ther.
8, 2296-2307
|Abstract »|Full Text »|PDF »
Activation of the Akt-NF-{kappa}B Pathway by Subtilase Cytotoxin through the ATF6 Branch of the Unfolded Protein Response.
H. Yamazaki, N. Hiramatsu, K. Hayakawa, Y. Tagawa, M. Okamura, R. Ogata, T. Huang, S. Nakajima, J. Yao, A. W. Paton, et al. (2009)
J. Immunol.
183, 1480-1487
|Abstract »|Full Text »|PDF »
The Degree of Folding Instability of the Envelope Protein of a Neurovirulent Murine Retrovirus Correlates with the Severity of the Neurological Disease.
J. L. Portis, P. Askovich, J. Austin, Y. Gutierrez-Cotto, and F. J. McAtee (2009)
J. Virol.
83, 6079-6086
|Abstract »|Full Text »|PDF »
Dehydrocostuslactone, a Medicinal Plant-Derived Sesquiterpene Lactone, Induces Apoptosis Coupled to Endoplasmic Reticulum Stress in Liver Cancer Cells.
Y.-L. Hsu, L.-Y. Wu, and P.-L. Kuo (2009)
J. Pharmacol. Exp. Ther.
329, 808-819
|Abstract »|Full Text »|PDF »
