duan-sch9regulatesintracellular-2015.pdf (2.24 MB)
Sch9 regulates intracellular protein ubiquitination by controlling stress responses
journal contribution
posted on 2015-08-01, 00:00 authored by B Qie, Z Lyu, L Lyu, J Liu, X Gao, Y Liu, Wei DuanWei Duan, N Zhang, L Du, K LiuProtein 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.
History
Journal
Redox biologyVolume
5Pagination
290 - 300Publisher
ElsevierLocation
Amsterdam, The NetherlandsPublisher DOI
Link to full text
ISSN
2213-2317eISSN
2213-2317Language
engPublication classification
C1 Refereed article in a scholarly journal; C Journal articleCopyright notice
2015, ElsevierUsage metrics
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