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.
CITATION STYLE
Rodriguez, J., Haydinger, C. D., Peet, D. J., Nguyen, L. K., & von Kriegsheim, A. (2020). Asparagine Hydroxylation is a Reversible Post-translational Modification. Molecular and Cellular Proteomics, 19(11), 1777–1789. https://doi.org/10.1074/mcp.RA120.002189
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