Asparagine Hydroxylation is a Reversible Post-translational Modification

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

Research output: Contribution to journalArticleResearchpeer-review

3 Citations (Scopus)

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 languageEnglish
Pages (from-to)1777-1789
Number of pages13
JournalMolecular & Cellular Proteomics
Volume19
Issue number11
DOIs
Publication statusPublished - 1 Nov 2020

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