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.

泛素特异性蛋白酶 (USP7)，也称为疱疹病毒相关泛素特异性蛋白酶 (HAUSP)，是一种去泛素酶。在发现 USP7 是 p53-MDM2 通路的关键调节因子后，USP7 最近受到了极大的关注。 USP7 蛋白大小为 130 kDa，具有多个可与多种蛋白质结合的结构域。这些相互作用介导关键的发育和稳态过程，包括细胞周期、免疫反应以及转录因子和表观遗传调节剂活性和定位的调节。 USP7 还通过 Wnt 信号通路的异常激活和 HIF-1α 的稳定促进癌发生。这些发现表明 USP7 可能诱导肿瘤进展并成为治疗靶点。加上对开发 USP7 作为靶点的兴趣，一些研究已经定义了新的蛋白质相互作用和 USP7 功能的调控网络。在这篇综述中，我们重点关注 USP7 的蛋白质相互作用，这对于其与癌症相关的作用最为重要。