Mdm2 binds p73α without targeting degradation
Mdm2 binds p73α without targeting degradation
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DOI：
10.1038/sj.onc.1202781
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发表时间：
1999-07-08
期刊：
影响因子：
8
通讯作者：
Vousden, KH
中科院分区：
文献类型：
--
作者：
Bálint, E;Bates, S;Vousden, KH
P53肿瘤抑制蛋白的功能是通过与MDM2的相互作用来调节的，MDM2针对P53进行泛素依赖的降解。我们在这里表明，像p53一样，p73α在体外和细胞内都与MDM2形成相互作用，但这不会导致p73α蛋白的降解。人乳头瘤病毒E6蛋白也不能降解p73α，这表明控制p73α稳定性的机制与已知的调控p53稳定性的机制是不同的。然而，MDM2与73α的相互作用足以阻碍p73α的转录功能，尽管没有降解。
The function of the p53 tumor suppressor protein is regulated by interaction with Mdm2, which targets p53 for ubiquitin dependent degradation. We show here that like p53, p73 alpha forms an interaction with Mdm2, both in vitro and in cells, but this does not result in the degradation of the p73 alpha protein. The human papillomavirus E6 protein also fails to degrade p73 alpha, suggesting that the mechanisms governing p73 alpha stability are distinct from those known to regulate p53 stability. However, the interaction of Mdm2 with 73 alpha is sufficient to impede p73 alpha transcriptional function, despite the lack of degradation.