细胞内稳态或肿瘤发生:USP7扮演双重代理人

M. Ghosh, Bhaskar Basu, Gouranga Saha, Shreyasee Ghatak Choudhury
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引用次数: 2

摘要

泛素特异性蛋白酶USP7/HAUSP是一种主要的去泛素酶,作用于广泛的底物蛋白。USP7的去泛素化通常会导致底物的稳定和蛋白酶体降解,但也会导致其细胞内定位和活性的改变。在其底物蛋白的基础上,USP7已被证明调节涉及维持体内平衡和促进肿瘤发生的过程。到目前为止,USP7似乎并不是这两种细胞现象的专门调节器,相反,一组特定底物相对于另一组底物的相对丰度是决定它将垄断哪种现象的因素。不幸的是,癌症的发生产生了大量的促癌底物,这导致USP7功能的急剧垄断,从而进一步增强促癌信号传导。
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Cellular Homeostasis or Tumorigenesis: USP7 Playing the Double Agent
The ubiquitin specific protease USP7/HAUSP is a major deubiquitinase that acts upon a wide spectrum of substrate proteins. Deubiquitination by USP7 generally leads to stabilization of substrates and their rescue from proteasomal degradation, but can also lead to alteration in their intracellular localization and activity. On the basis of its substrate proteins, USP7 has been shown to regulate processes involved in both the maintenance of homeostasis and the promotion of tumorigenesis. USP7, so far does not seem to be a dedicated regulator for either of these cellular phenomena, instead the relative abundance of a particular set of substrates over another being the factor that decides towards which phenomena it will be monopolized. The onset of cancer unfortunately creates an abundance of pro-oncogenic substrates, and this leads to a drastic monopolization of USP7 function towards the enhancement of further pro-oncogenic signaling.
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