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首页> 外文期刊>EMBO Journal >An essential function of the extreme C-terminus of MDM2 can be provided by MDMX
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An essential function of the extreme C-terminus of MDM2 can be provided by MDMX

机译:一个重要的极端糖基的函数MDM2可由MDMX提供

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摘要

tumor suppressor protein for degradation. The RING domain is essential for the E3 activity of MDM2, and we show here that the extreme C-terminal tail of MDM2 is also critical for efficient E3 activity. Loss of E3 function in MDM2 mutants deleted of the C-terminal tail correlated with a failure of these mutants to oligomerize with MDM2, or with the related protein MDMX (HDMX). However, MDM2 containing point mutations within the C-terminus that inactivated E3 function retained the ability to oligomerize with the wild-type MDM2 RING domain and MDMX, and our results indicate that oligomers containing both wild-type MDM2 and a C-terminal mutant protein retain E3 function both in auto-degradation and degradation of p53. Interestingly, the E3 activity of C-terminal point mutants of MDM2 can also be supported by interaction with wild-type MDMX, suggesting that MDMX can directly contribute to E3 function.
机译:肿瘤抑制蛋白降解。域对MDM2的E3活动至关重要,这里显示,极端的c端尾对于有效的E3 MDM2也是至关重要的活动。删除的c端尾部相关这些突变体oligomerize的失败MDM2、或相关蛋白质MDMX (HDMX)。然而,MDM2包含点突变灭活E3的糖基函数保留了oligomerize与能力野生型MDM2环域和MDMX和我们结果表明,低聚物包含两种野生型MDM2和c端突变蛋白保留E3 auto-degradation和函数p53的退化。MDM2 c端点突变体的活动与野生型也是支持的交互MDMX,表明MDMX可以直接为E3函数。

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