Asparagine Hydroxylation is a Reversible Post-translational Modification.

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.

SUBMITTER: Rodriguez J 

PROVIDER: S-EPMC7664127 | biostudies-literature | 2020 Nov

REPOSITORIES: biostudies-literature