期刊
EMBO REPORTS
卷 16, 期 9, 页码 1131-1144出版社
WILEY
DOI: 10.15252/embr.201540298
关键词
oxidative stress; phosphorylation; protein turnover; proteomics; ubiquitin
资金
- NIH/NCI grant [R00CA140789]
- Ellison Medical Foundation New Scholar Award [AG-NS- 0953-12]
Ubiquitylation is an essential post-translational modification that regulates numerous cellular processes, most notably protein degradation. Ubiquitin can itself be phosphorylated at nearly every serine, threonine, and tyrosine residue. However, the effect of this modification on ubiquitin function is largely unknown. Here, we characterized the effects of phosphorylation of yeast ubiquitin at serine 65 invivo and invitro. We find this post-translational modification to be regulated under oxidative stress, occurring concomitantly with the restructuring of the ubiquitin landscape into a highly polymeric state. Phosphomimetic mutation of S65 recapitulates the oxidative stress phenotype, causing a dramatic accumulation of ubiquitylated proteins and a proteome-wide reduction of protein turnover rates. Importantly, this mutation impacts ubiquitin chain disassembly, chain linkage distribution, ubiquitin interactions, and substrate targeting. These resultsdemonstrate that phosphorylation is an additional mode of ubiquitin regulation with broad implications in cellular physiology.
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