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Sch9 regulates intracellular protein ubiquitination by controlling stress responses.

ABSTRACT: 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 sch9? 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.

SUBMITTER: Qie B

PROVIDER: S-EPMC4477112 | biostudies-literature | 2015 Aug

REPOSITORIES: biostudies-literature

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Sch9 regulates intracellular protein ubiquitination by controlling stress responses.

Qie Beibei B Lyu Zhou Z Lyu Lei L Liu Jun J Gao Xuejie X Liu Yanyan Y Duan Wei W Zhang Nianhui N Du Linfang L Liu Ke K

Redox biology 20150609

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 ...[more]

PMID: 26087116

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Project description:This SuperSeries is composed of the SubSeries listed below.

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