共查询到20条相似文献，搜索用时 15 毫秒
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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. 相似文献
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Toh WH Siddique MM Boominathan L Lin KW Sabapathy K 《The Journal of biological chemistry》2004,279(43):44713-44722
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L Raycroft J R Schmidt K Yoas M M Hao G Lozano 《Molecular and cellular biology》1991,11(12):6067-6074
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Cdk5 phosphorylates p53 and regulates its activity 总被引：2，自引：0，他引：2
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Peidis P Voukkalis N Aggelidou E Georgatsou E Hadzopoulou-Cladaras M Scott RE Nikolakaki E Giannakouros T 《FEBS letters》2011,585(1):78-84
A significant amount of nuclear p53 is found associated with the nuclear matrix in cells that were exposed to genotoxic stress. In this study we identified Scaffold attachment factor B1 (SAFB1), a nuclear matrix-associated protein that binds the scaffold or matrix attachment regions (S/MARs) of genomic DNA, as a novel p53-interacting protein. SAFB1 was able to associate with p53 through its C-terminal domain, while significant co-localization of the two proteins was observed in cells treated with 5-fluorouracil or mithramycin. Binding of p53 to SAFB1 had a significant functional outcome, since SAFB1 was shown to suppress p53-mediated reporter gene expression. These data suggest that nuclear matrix-associated proteins may play a critical role in regulating p53 localization and activity.