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. 2006 Oct;8(10):1074-83.
doi: 10.1038/ncb1470. Epub 2006 Sep 10.

Modification of p53 with O-linked N-acetylglucosamine regulates p53 activity and stability

Won Ho Yang  1 , Ji Eun Kim, Hyung Wook Nam, Jung Won Ju, Hoe Suk Kim, Yu Sam Kim, Jin Won Cho
Affiliations

Modification of p53 with O-linked N-acetylglucosamine regulates p53 activity and stability

Won Ho Yang et al. Nat Cell Biol. 2006 Oct.

Erratum in

  • Nat Cell Biol. 2007 Dec;9(12):1442

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.

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