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Asparagine hydroxylation is likely to be a reversible post-translational modification

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

Posted 25 Mar 2020
bioRxiv DOI: 10.1101/2020.03.22.002436

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.

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