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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 (Ubiquitin-specific protease 2, USP2) is an important deubiquitinating enzyme that targets deproteinized cells by specifically recognizing the target protein, deubiquitinating the target protein and inhibiting its degradation to regulate intracellular Target protein quantity and activity, and thus participate in the regulation of cell function. USP2-45 and USP2-69 are two different subtypes formed by alternative splicing of USP2 gene, which are expressed in different tissues, cells and different developmental stages, and are closely related to cell cycle regulation, longitudinal growth of skeletal muscle, differentiation of muscle cells, Ion channels, spermatogenesis and biological clock regulation and other closely related. Based on the current research progress, this article systematically elaborates the structure, distribution and function of the two subtypes of USP2, laying a theoretical foundation for further study on the relationship between USP2 and the disease.