Article
Phosphorylation of ubiquitin at Ser65 affects its polymerization, targets, and proteome-wide turnover.
EMBO reports - 1 Sept 2015
Swaney Danielle L, Rodríguez-Mias Ricard A, Villén Judit
Abstract excerpt
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 in vivo...
Topics
- Cell Survival
- Mass Spectrometry
- Mutation
- Oxidative Stress
- Phosphorylation
- Polymerization
- Protein Interaction Domains and Motifs
- Protein Processing, Post-Translational
- Proteome
- Proteomics
- Saccharomyces cerevisiae
- Saccharomyces cerevisiae Proteins
- Stress, Physiological
- Ubiquitin
- Ubiquitination