Asparagine Hydroxylation is a Reversible Post-translational Modification.
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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 signaling networks, such as phosphorylation, methylation and ubiquitylation.
SUBMITTER: Rodriguez J
PROVIDER: S-EPMC7664127 | biostudies-literature |
REPOSITORIES: biostudies-literature
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