Sch9 regulates intracellular protein ubiquitination by controlling stress responses

3Citations
Citations of this article
26Readers
Mendeley users who have this article in their library.

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 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.

Cite

CITATION STYLE

APA

Qie, B., Lyu, Z., Lyu, L., Liu, J., Gao, X., Liu, Y., … Liu, K. (2015). Sch9 regulates intracellular protein ubiquitination by controlling stress responses. Redox Biology, 5, 290–300. https://doi.org/10.1016/j.redox.2015.06.002

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free