Asparagine Hydroxylation is a Reversible Post-translational Modification
2020 ◽
Vol 19
(11)
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pp. 1777-1789
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Keyword(s):
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.
1990 ◽
Vol 45
(9-10)
◽
pp. 987-998
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2018 ◽
Vol 13
(5)
◽
pp. 1137-1141
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1991 ◽
Vol 266
(13)
◽
pp. 8102-8107