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

Rodriguez, J.; Haydinger, C. D.; Peet, D.; Nguyen, L.; von Kriegsheim, A.

doi:10.1101/2020.03.22.002436

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bioRxiv · 10.1101/2020.03.22.002436

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

Rodriguez, J.·Haydinger, C. D.·Peet, D.·Nguyen, L.·von Kriegsheim, A.

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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.

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Rodriguez, J., Haydinger, C. D., Peet, D., Nguyen, L., von Kriegsheim, A.. 2020-03-25. Asparagine hydroxylation is likely to be a reversible post-translational modification. https://doi.org/10.1101/2020.03.22.002436

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