IRE1 signaling affects cell fate during the unfolded protein response
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...
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| Published in: | Science (American Association for the Advancement of Science) Vol. 318; no. 5852; p. 944 |
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| Main Authors: | , , , , , , , , |
| Format: | Journal Article |
| Language: | English |
| Published: |
United States
09.11.2007
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| Subjects: | |
| ISSN: | 1095-9203, 1095-9203 |
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| 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. |
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| AbstractList | 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. 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.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. |
| Author | Shokat, Kevan M Lin, Jonathan H Panning, Barbara Zhang, Chao Li, Han Cohen, Hannah R Walter, Peter Lavail, Matthew M Yasumura, Douglas |
| Author_xml | – sequence: 1 givenname: Jonathan H surname: Lin fullname: Lin, Jonathan H email: Jonathan.Lin@ucsf.edu organization: Howard Hughes Medical Institute, University of California at San Francisco, San Francisco, CA 94158, USA. Jonathan.Lin@ucsf.edu – sequence: 2 givenname: Han surname: Li fullname: Li, Han – sequence: 3 givenname: Douglas surname: Yasumura fullname: Yasumura, Douglas – sequence: 4 givenname: Hannah R surname: Cohen fullname: Cohen, Hannah R – sequence: 5 givenname: Chao surname: Zhang fullname: Zhang, Chao – sequence: 6 givenname: Barbara surname: Panning fullname: Panning, Barbara – sequence: 7 givenname: Kevan M surname: Shokat fullname: Shokat, Kevan M – sequence: 8 givenname: Matthew M surname: Lavail fullname: Lavail, Matthew M – sequence: 9 givenname: Peter surname: Walter fullname: Walter, Peter |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/17991856$$D View this record in MEDLINE/PubMed |
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| SubjectTerms | Activating Transcription Factor 6 - metabolism Animals Animals, Genetically Modified Apoptosis Cell Line Cell Survival Disease Models, Animal eIF-2 Kinase - metabolism Endoplasmic Reticulum - metabolism Endoribonucleases - genetics Endoribonucleases - metabolism Humans Kinetics Membrane Proteins - genetics Membrane Proteins - metabolism Mice Mutation Protein Folding Protein Serine-Threonine Kinases - genetics Protein Serine-Threonine Kinases - metabolism Proteins - chemistry Proteins - metabolism Rats Retina - metabolism Retinitis Pigmentosa - metabolism Rhodopsin - chemistry Rhodopsin - metabolism Signal Transduction |
| Title | IRE1 signaling affects cell fate during the unfolded protein response |
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