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Sch9 regulates intracellular protein ubiquitination by controlling stress responses
Protein ubiquitination and the subsequent degradation are important means by which aberrant proteins are removed from cells, a key requirement for long-term survival. In this study, we found that the overall level of ubiquitinated proteins dramatically decreased as yeast cell grew from log to statio...
Autores principales: | , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Elsevier
2015
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4477112/ https://www.ncbi.nlm.nih.gov/pubmed/26087116 http://dx.doi.org/10.1016/j.redox.2015.06.002 |
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author | Qie, Beibei Lyu, Zhou Lyu, Lei Liu, Jun Gao, Xuejie Liu, Yanyan Duan, Wei Zhang, Nianhui Du, Linfang Liu, Ke |
author_facet | Qie, Beibei Lyu, Zhou Lyu, Lei Liu, Jun Gao, Xuejie Liu, Yanyan Duan, Wei Zhang, Nianhui Du, Linfang Liu, Ke |
author_sort | Qie, Beibei |
collection | PubMed |
description | Protein ubiquitination and the subsequent degradation are important means by which aberrant proteins are removed from cells, a key requirement for long-term survival. In this study, we found that the overall level of ubiquitinated proteins dramatically decreased as yeast cell grew from log to stationary phase. Deletion of SCH9, a gene encoding a key protein kinase for longevity control, decreased the level of ubiquitinated proteins in log phase and this effect could be reversed by restoring Sch9 function. We demonstrate here that the decrease of ubiquitinated proteins in sch9Δ cells in log phase is not caused by changes in ubiquitin expression, proteasome activity, or autophagy, but by enhanced expression of stress response factors and a decreased level of oxidative stress. Our results revealed for the first time how Sch9 regulates the level of ubiquitinated proteins and provides new insight into how Sch9 controls longevity. |
format | Online Article Text |
id | pubmed-4477112 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | Elsevier |
record_format | MEDLINE/PubMed |
spelling | pubmed-44771122015-06-24 Sch9 regulates intracellular protein ubiquitination by controlling stress responses Qie, Beibei Lyu, Zhou Lyu, Lei Liu, Jun Gao, Xuejie Liu, Yanyan Duan, Wei Zhang, Nianhui Du, Linfang Liu, Ke Redox Biol Article Protein ubiquitination and the subsequent degradation are important means by which aberrant proteins are removed from cells, a key requirement for long-term survival. In this study, we found that the overall level of ubiquitinated proteins dramatically decreased as yeast cell grew from log to stationary phase. Deletion of SCH9, a gene encoding a key protein kinase for longevity control, decreased the level of ubiquitinated proteins in log phase and this effect could be reversed by restoring Sch9 function. We demonstrate here that the decrease of ubiquitinated proteins in sch9Δ cells in log phase is not caused by changes in ubiquitin expression, proteasome activity, or autophagy, but by enhanced expression of stress response factors and a decreased level of oxidative stress. Our results revealed for the first time how Sch9 regulates the level of ubiquitinated proteins and provides new insight into how Sch9 controls longevity. Elsevier 2015-06-09 /pmc/articles/PMC4477112/ /pubmed/26087116 http://dx.doi.org/10.1016/j.redox.2015.06.002 Text en © 2015 The Authors http://creativecommons.org/licenses/by-nc-nd/4.0/ This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/). |
spellingShingle | Article Qie, Beibei Lyu, Zhou Lyu, Lei Liu, Jun Gao, Xuejie Liu, Yanyan Duan, Wei Zhang, Nianhui Du, Linfang Liu, Ke Sch9 regulates intracellular protein ubiquitination by controlling stress responses |
title | Sch9 regulates intracellular protein ubiquitination by controlling stress responses |
title_full | Sch9 regulates intracellular protein ubiquitination by controlling stress responses |
title_fullStr | Sch9 regulates intracellular protein ubiquitination by controlling stress responses |
title_full_unstemmed | Sch9 regulates intracellular protein ubiquitination by controlling stress responses |
title_short | Sch9 regulates intracellular protein ubiquitination by controlling stress responses |
title_sort | sch9 regulates intracellular protein ubiquitination by controlling stress responses |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4477112/ https://www.ncbi.nlm.nih.gov/pubmed/26087116 http://dx.doi.org/10.1016/j.redox.2015.06.002 |
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