The USP7 protein interaction network and its roles in tumorigenesis.
The USP7 protein interaction network and its roles in tumorigenesis.
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DOI：
10.1016/j.gendis.2020.10.004
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发表时间：
2022-01
期刊：
影响因子：
6.8
通讯作者：
Ewing RM
中科院分区：
文献类型：
--
作者：
Al-Eidan A;Wang Y;Skipp P;Ewing RM
泛素特异性蛋白酶（USP 7），也称为疱疹病毒相关泛素特异性蛋白酶（HAUSP），是一种去泛素化酶。在发现USP 7是p53-MDM 2途径的关键调节剂之后，最近对USP 7有显著的关注。USP 7蛋白的大小为130 kDa，具有多个结构域，可与多种蛋白质结合。这些相互作用介导关键的发育和稳态过程，包括细胞周期，免疫应答，转录因子和表观遗传调节因子活性和定位的调节。USP 7还通过Wnt信号通路的异常激活和HIF-1α的稳定化促进致癌作用。这些发现表明USP 7可能诱导肿瘤进展并成为治疗靶点。除了开发USP 7作为靶标的兴趣之外，一些研究已经定义了新的蛋白质相互作用和USP 7发挥功能的调控网络。在这篇综述中，我们重点介绍了USP 7的蛋白质相互作用，这对它的癌症相关作用至关重要。
Ubiquitin-specific protease (USP7), also known as Herpesvirus-associated ubiquitin-specific protease (HAUSP), is a deubiquitinase. There has been significant recent attention on USP7 following the discovery that USP7 is a key regulator of the p53-MDM2 pathway. The USP7 protein is 130 kDa in size and has multiple domains which bind to a diverse set of proteins. These interactions mediate key developmental and homeostatic processes including the cell cycle, immune response, and modulation of transcription factor and epigenetic regulator activity and localization. USP7 also promotes carcinogenesis through aberrant activation of the Wnt signalling pathway and stabilization of HIF-1α. These findings have shown that USP7 may induce tumour progression and be a therapeutic target. Together with interest in developing USP7 as a target, several studies have defined new protein interactions and the regulatory networks within which USP7 functions. In this review, we focus on the protein interactions of USP7 that are most important for its cancer-associated roles.
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