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- Publisher
- Springer Journals
- Copyright
- Copyright © 2006 by Nature Publishing Group
- Subject
- Life Sciences; Life Sciences, general; Cell Biology; Cancer Research; Developmental Biology; Stem Cells
- ISSN
- 1465-7392
- eISSN
- 1476-4679
- DOI
- 10.1038/ncb1470
- Publisher site
- See Article on Publisher Site
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.
Journal
Nature Cell Biology – Springer Journals
Published: Sep 10, 2006