Projects per year
Abstract
Amino acid hydroxylation is a common post-translational modification, which generally regulates protein interactions or adds a functional group that can be further modified. Such hydroxylation is currently considered irreversible, necessitating the degradation and re-synthesis of the entire protein to reset the modification. Here we present evidence that the cellular machinery can reverse FIH-mediated asparagine hydroxylation on intact proteins. These data suggest that asparagine hydroxylation is a flexible and dynamic post-translational modification akin to modifications involved in regulating signaling networks, such as phosphorylation, methylation and ubiquitylation.
Original language | English |
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Pages (from-to) | 1777-1789 |
Number of pages | 13 |
Journal | Molecular & Cellular Proteomics |
Volume | 19 |
Issue number | 11 |
DOIs | |
Publication status | Published - 1 Nov 2020 |
Projects
- 1 Active
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Combating adaptive resistance to tageted therapy in triple-negative breast cancer
Nguyen, L., Swarbrick, A., Richardson, G., Loi, S. & Daly, R.
15/02/19 → 14/02/23
Project: Research