磷酸化
蛋白质水解
泛素
细胞生物学
化学
脱磷
N-乙酰氨基葡萄糖
P53蛋白
生物化学
生物
磷酸酶
酶
细胞凋亡
基因
作者
Won Ho Yang,Ji Eun Kim,Hyung Wook Nam,Jung‐Won Ju,Hoe Suk Kim,Yu Sam Kim,Jin Won Cho
摘要
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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