Cargando…
Putting the brakes on the unfolded protein response
The unfolded protein response is an ancient cellular pathway for rapidly responding to endoplasmic reticulum stress. Two studies in this issue (Rubio et al. 2011. J. Cell. Biol. doi:10.1083/jcb.201007077 and Chawla et al. 2011. J. Cell. Biol. doi:10.1083/jcb.201008071) provide insight into how the u...
Autores principales: | , |
---|---|
Formato: | Texto |
Lenguaje: | English |
Publicado: |
The Rockefeller University Press
2011
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3082173/ https://www.ncbi.nlm.nih.gov/pubmed/21444688 http://dx.doi.org/10.1083/jcb.201101105 |
_version_ | 1782202269799809024 |
---|---|
author | Sicheri, Frank Silverman, Robert H. |
author_facet | Sicheri, Frank Silverman, Robert H. |
author_sort | Sicheri, Frank |
collection | PubMed |
description | The unfolded protein response is an ancient cellular pathway for rapidly responding to endoplasmic reticulum stress. Two studies in this issue (Rubio et al. 2011. J. Cell. Biol. doi:10.1083/jcb.201007077 and Chawla et al. 2011. J. Cell. Biol. doi:10.1083/jcb.201008071) provide insight into how the unfolded protein response is tamped down to restore normal endoplasmic reticulum function. Although both papers implicate the Ire1 kinase domain as the key effector of the off-switch mechanism, alternate models for how this is achieved are proposed. |
format | Text |
id | pubmed-3082173 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2011 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-30821732011-10-04 Putting the brakes on the unfolded protein response Sicheri, Frank Silverman, Robert H. J Cell Biol Reviews The unfolded protein response is an ancient cellular pathway for rapidly responding to endoplasmic reticulum stress. Two studies in this issue (Rubio et al. 2011. J. Cell. Biol. doi:10.1083/jcb.201007077 and Chawla et al. 2011. J. Cell. Biol. doi:10.1083/jcb.201008071) provide insight into how the unfolded protein response is tamped down to restore normal endoplasmic reticulum function. Although both papers implicate the Ire1 kinase domain as the key effector of the off-switch mechanism, alternate models for how this is achieved are proposed. The Rockefeller University Press 2011-04-04 /pmc/articles/PMC3082173/ /pubmed/21444688 http://dx.doi.org/10.1083/jcb.201101105 Text en © 2011 Sicheri and Silverman This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/). |
spellingShingle | Reviews Sicheri, Frank Silverman, Robert H. Putting the brakes on the unfolded protein response |
title | Putting the brakes on the unfolded protein response |
title_full | Putting the brakes on the unfolded protein response |
title_fullStr | Putting the brakes on the unfolded protein response |
title_full_unstemmed | Putting the brakes on the unfolded protein response |
title_short | Putting the brakes on the unfolded protein response |
title_sort | putting the brakes on the unfolded protein response |
topic | Reviews |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3082173/ https://www.ncbi.nlm.nih.gov/pubmed/21444688 http://dx.doi.org/10.1083/jcb.201101105 |
work_keys_str_mv | AT sicherifrank puttingthebrakesontheunfoldedproteinresponse AT silvermanroberth puttingthebrakesontheunfoldedproteinresponse |