Rxivist logo

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.

Download data

  • Downloaded 311 times
  • Download rankings, all-time:
    • Site-wide: 104,036
    • In biochemistry: 3,056
  • Year to date:
    • Site-wide: 104,174
  • Since beginning of last month:
    • Site-wide: 83,004

Altmetric data

Downloads over time

Distribution of downloads per paper, site-wide