去泛素化酶USP3在细胞中的功能作用及其研究进展

The Molecular Function of Deubiquitinating Enzyme USP3 in Cell and Its Research Progress

Ubiquitin-specific protease 3（USP3）属于半胱氨酸蛋白酶,是去泛素化酶家族（deubiquitinating enzymes,DUBs）的重要成员,为能够断裂脯氨酸残基连接的泛素链的特异性蛋白酶。USP3蛋白由520 aa组成,有两个保守的蛋白结构域：一个为催化结构域,即泛素特异性蛋白酶活性区域,另一个为锌指泛素连接结构域（Zn F-UBP）即泛素连接区。近年来研究表明USP3参与细胞中多种生命活动的调节,如细胞增殖、细胞周期、DNA损伤修复等。同时,USP3在炎症应答及肝癌的发生发展中也表现出重要的作用。本综述就USP3在细胞中的功能作用以及最新研究进展进行了综述。

Ubiquitin-specific protease 3 （USP3）, a cysteine protease, is an important member of the deubiquitinating enzyme family. USP3 is able to efficiently cleave the ubiquitin-proline bond. The USP3 protein consists of 520 aa and has two conserved protein domains： a catalytic domain of the Ub-specific protease （USP） class and a zinc finger （ZnF-UBP） Ub-binding domain. Recent studies have revealed that USP3 is involved in the regulation of multiple cellular biological processes, such as cell proliferation, cell cycle, DNA damage repair and so on. Meanwhile, USP3 plays key roles in inflammation response and liver cancer. Here, we review the function and the latest research progress of USP3 in the cell.