Sir2 histone deacetylase prevents programmed cell death caused by sustained activation of the Hog1 stress-activated protein kinase
Exposure of yeast to high osmolarity induces a transient activation of the Hog1 stress-activated protein kinase (SAPK), which is required for cell survival under these conditions. However, sustained activation of the SAPK results in a severe growth defect. We found that prolonged SAPK activation lea...
| Autores: | , , , , , , |
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| Tipo de recurso: | artículo |
| Estado: | Versión publicada |
| Fecha de publicación: | 2011 |
| País: | España |
| Institución: | Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya) |
| Repositorio: | Recercat. Dipósit de la Recerca de Catalunya |
| OAI Identifier: | oai:recercat.cat:10230/25460 |
| Acceso en línea: | http://hdl.handle.net/10230/25460 http://dx.doi.org/10.1038/embor.2011.154 |
| Access Level: | acceso abierto |
| Palabra clave: | Saccharomyces cerevisiae -- Metabolisme Factors de transcripció Proteïnes |
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Sir2 histone deacetylase prevents programmed cell death caused by sustained activation of the Hog1 stress-activated protein kinaseVendrell Arasa, AlexandreMartínez Pastor, MarGonzález Novo, AlbertoPascual Ahuir, AmparoSinclair, David A.Proft, MarkusPosas Garriga, FrancescSaccharomyces cerevisiae -- MetabolismeFactors de transcripcióProteïnesExposure of yeast to high osmolarity induces a transient activation of the Hog1 stress-activated protein kinase (SAPK), which is required for cell survival under these conditions. However, sustained activation of the SAPK results in a severe growth defect. We found that prolonged SAPK activation leads to cell death, which is not observed in nma111 cells, by causing accumulation of reactive oxygen species (ROS). Mutations of the SCF(CDC4) ubiquitin ligase complex suppress cell death by preventing the degradation of Msn2 and Msn4 transcription factors. Accumulation of Msn2 and Msn4 leads to the induction of PNC1, which is an activator of the Sir2 histone acetylase. Sir2 is involved in protection against Hog1-induced cell death and can suppress Hog1-induced ROS accumulation. Therefore, cell death seems to be dictated by the balance of ROS induced by Hog1 and the protective effect of Sir2.This work was supported by grants from the Ministerio de Ciència y Innovación (BIO2009-07762) and Consolider Ingenio 2010 programme (grant CSD2007-0015), UNICELLSYS from FP7, as well as supported byFundación Marcelino Botín. F.P. is the recipient of the Institució Catalana de Recerca i Estudis Avançats Acadèmia (Generalitat de Catalunya). D.A.S. is supported by grants from the National Institute on Aging National Institutes of Health, the Ellison Medical Foundation and the Glenn Foundation for Medical Research.Nature Publishing Group201520152011info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionapplication/pdfapplication/pdfhttp://hdl.handle.net/10230/25460http://dx.doi.org/10.1038/embor.2011.154reponame:Recercat. Dipósit de la Recerca de Catalunyainstname:Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)InglésEMBO reports. 2011;12(10):1062-608info:eu-repo/grantAgreement/ES/3PN/BIO2009-07762© Nature Publishing Group. http://dx.doi.org/10.1038/embor.2011.154. This work is licensed under a Creative Commons Attribution-NonCommercial-Share Alike 3.0 Unported licencehttp://creativecommons.org/licenses/by-nc-sa/3.0/info:eu-repo/semantics/openAccessoai:recercat.cat:10230/254602026-05-29T05:05:01Z |
| dc.title.none.fl_str_mv |
Sir2 histone deacetylase prevents programmed cell death caused by sustained activation of the Hog1 stress-activated protein kinase |
| title |
Sir2 histone deacetylase prevents programmed cell death caused by sustained activation of the Hog1 stress-activated protein kinase |
| spellingShingle |
Sir2 histone deacetylase prevents programmed cell death caused by sustained activation of the Hog1 stress-activated protein kinase Vendrell Arasa, Alexandre Saccharomyces cerevisiae -- Metabolisme Factors de transcripció Proteïnes |
| title_short |
Sir2 histone deacetylase prevents programmed cell death caused by sustained activation of the Hog1 stress-activated protein kinase |
| title_full |
Sir2 histone deacetylase prevents programmed cell death caused by sustained activation of the Hog1 stress-activated protein kinase |
| title_fullStr |
Sir2 histone deacetylase prevents programmed cell death caused by sustained activation of the Hog1 stress-activated protein kinase |
| title_full_unstemmed |
Sir2 histone deacetylase prevents programmed cell death caused by sustained activation of the Hog1 stress-activated protein kinase |
| title_sort |
Sir2 histone deacetylase prevents programmed cell death caused by sustained activation of the Hog1 stress-activated protein kinase |
| dc.creator.none.fl_str_mv |
Vendrell Arasa, Alexandre Martínez Pastor, Mar González Novo, Alberto Pascual Ahuir, Amparo Sinclair, David A. Proft, Markus Posas Garriga, Francesc |
| author |
Vendrell Arasa, Alexandre |
| author_facet |
Vendrell Arasa, Alexandre Martínez Pastor, Mar González Novo, Alberto Pascual Ahuir, Amparo Sinclair, David A. Proft, Markus Posas Garriga, Francesc |
| author_role |
author |
| author2 |
Martínez Pastor, Mar González Novo, Alberto Pascual Ahuir, Amparo Sinclair, David A. Proft, Markus Posas Garriga, Francesc |
| author2_role |
author author author author author author |
| dc.subject.none.fl_str_mv |
Saccharomyces cerevisiae -- Metabolisme Factors de transcripció Proteïnes |
| topic |
Saccharomyces cerevisiae -- Metabolisme Factors de transcripció Proteïnes |
| description |
Exposure of yeast to high osmolarity induces a transient activation of the Hog1 stress-activated protein kinase (SAPK), which is required for cell survival under these conditions. However, sustained activation of the SAPK results in a severe growth defect. We found that prolonged SAPK activation leads to cell death, which is not observed in nma111 cells, by causing accumulation of reactive oxygen species (ROS). Mutations of the SCF(CDC4) ubiquitin ligase complex suppress cell death by preventing the degradation of Msn2 and Msn4 transcription factors. Accumulation of Msn2 and Msn4 leads to the induction of PNC1, which is an activator of the Sir2 histone acetylase. Sir2 is involved in protection against Hog1-induced cell death and can suppress Hog1-induced ROS accumulation. Therefore, cell death seems to be dictated by the balance of ROS induced by Hog1 and the protective effect of Sir2. |
| publishDate |
2011 |
| dc.date.none.fl_str_mv |
2011 2015 2015 |
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info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion |
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article |
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publishedVersion |
| dc.identifier.none.fl_str_mv |
http://hdl.handle.net/10230/25460 http://dx.doi.org/10.1038/embor.2011.154 |
| url |
http://hdl.handle.net/10230/25460 http://dx.doi.org/10.1038/embor.2011.154 |
| dc.language.none.fl_str_mv |
Inglés |
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Inglés |
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EMBO reports. 2011;12(10):1062-608 info:eu-repo/grantAgreement/ES/3PN/BIO2009-07762 |
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http://creativecommons.org/licenses/by-nc-sa/3.0/ info:eu-repo/semantics/openAccess |
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http://creativecommons.org/licenses/by-nc-sa/3.0/ |
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openAccess |
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application/pdf application/pdf |
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Nature Publishing Group |
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Nature Publishing Group |
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reponame:Recercat. Dipósit de la Recerca de Catalunya instname:Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya) |
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