泛素特异性加工酶2的研究进展

Research progress in ubiquitin-specific protease 2

泛素特异性加工酶2(ubiquitin-specific protease 2,USP2)是一种重要的去泛素化酶,通过特异性识别靶蛋白,使靶蛋白去泛素化并阻碍其降解,以调控细胞内靶蛋白数量和活性,从而参与细胞功能的调节。USP2-45及USP2-69是USP2基因选择性剪接而形成的两种不同亚型,在不同组织、细胞和不同发育阶段均有表达,且与细胞周期调控,骨骼肌纵向生长、肌细胞分化、离子通道、生精作用及生物钟调控等关系密切。本文结合当前研究进展,系统阐述USP2的两种亚型的结构、分布及功能,为进一步研究USP2与疾病的关系打下理论基础。

Ubiquitin-specific protease 2（USP2） is an important de-ubiquitinating enzyme.By identifying the target protein specifically,USP2 can de-ubiquitinate the target protein and protect it from degradation,through which to regulate the number and activity of many intracellular proteins and in turn to modulate cellular function.Present studies demonstrate that USP2-69 and USP2-45 are two isoforms of USP2 by alternate splicing.Both USP2-69 and USP2-45 can be expressed in different cells and tissues in different stages of development.The current studies on USP2 are focused on its role in regulation of the cell cycle,skeletal muscle stretch,myogenesis,the function of epithelial Na channel（ENaC）,KCNQ1 potassium channel,and so on.This review focuses on the structure,tissue distribution,cellular localization and function of USP2（including its two isoforms）,which pave the way for the further research on USP2 and diseases.