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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >The E3 ubiquitin ligase Itch controls the protein stability of p63
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The E3 ubiquitin ligase Itch controls the protein stability of p63

机译：E3泛素连接酶Itch控制p63的蛋白质稳定性

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摘要

p63, a member of the p53 family of transcription factors, plays an important role in epithelial development, regulating both cell cycle and apoptosis. Even though p63 activity is regulated mainly at the posttranslational level, the control of p63 protein stability is far from being fully understood. Here, we show that the Hect (homologous to the E6-associated protein C terminus)-containing Nedd4-like ubiquitin protein ligase Itch binds, ubiquitylates, and promotes the degradation of p63. The physical interaction occurs at the border between the PY and the SAM (sterile a motif) domains; a single Y504F mutation significantly affects p63 degradation. Itch and p63 are coexpressed in the epidermis and in primary keratinocytes where Itch controls the p63 protein steady-state level. Accordingly, p63 protein levels are significantly increased in Itch knockout keratinocytes. These data suggest that Itch has a fundamental role in the mechanism that controls endogenous p63 protein levels and therefore contributes to regulation of p63 in physiological conditions.
机译：p63是转录因子p53家族的成员，在上皮发育中起着重要作用，同时调节细胞周期和细胞凋亡。即使p63活性主要在翻译后水平上进行调节，对p63蛋白稳定性的控制仍远未完全了解。在这里，我们显示含有Hed（与E6相关的蛋白C末端同源）的Nedd4样泛素蛋白连接酶Itch结合，泛素化并促进p63的降解。物理相互作用发生在PY和SAM（无菌基序）域之间的边界处；一个单一的Y504F突变会明显影响p63降解。 Itch和p63在表皮和原发性角质形成细胞中共表达，在那里Itch控制着p63蛋白的稳态水平。因此，在Itch敲除角质形成细胞中p63蛋白水平显着增加。这些数据表明，瘙痒在控制内源性p63蛋白水平的机制中具有根本作用，因此有助于在生理条件下调节p63。

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