We found a match
Your institution may have access to this item. Find your institution then sign in to continue.
- Title
Modification of p53 with O-linked N-acetylglucosamine regulates p53 activity and stability.
- Authors
Yang, Won Ho; Kim, Ji Eun; Nam, Hyung Wook; Ju, Jung Won; Kim, Hoe Suk; Kim, Yu Sam; Cho, Jin Won
- Abstract
Post-translational addition of O-linked N-acetylglucosamine (O-GlcNAc) to p53 is known to occur, but the site of O-GlcNAcylation and its effects on p53 are not understood. Here, we show that Ser 149 of p53 is O-GlcNAcylated and that this modification is associated with decreased phosphorylation of p53 at Thr 155, which is a site that is targeted by the COP9 signalosome, resulting in decreased p53 ubiquitination. Accordingly, O-GlcNAcylation at Ser 149 stabilizes p53 by blocking ubiquitin-dependent proteolysis. Our results indicate that the dynamic interplay between O-GlcNAc and O-phosphate modifications coordinately regulate p53 stability and activity.
- Subjects
GLUCOSAMINE; ACYLATION; PHOSPHORYLATION; PROTEOLYSIS; PROTEIN kinases; ATAXIA telangiectasia; DOXORUBICIN
- Publication
Nature Cell Biology, 2006, Vol 8, Issue 10, p1074
- ISSN
1465-7392
- Publication type
Article
- DOI
10.1038/ncb1470