Asparagine hydroxylation is a reversible post-translational modification

Javier Rodriguez Martinez, Cameron D Haydinger, Daniel J. Peet, Lan K Nguyen, Alex von Kriegsheim

Research output: Contribution to journalArticlepeer-review

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 signalling networks, such as phosphorylation, methylation and ubiquitylation.
Original languageEnglish
JournalMolecular and Cellular Proteomics
Early online date5 Aug 2020
DOIs
Publication statusE-pub ahead of print - 5 Aug 2020

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