PDF(Pubmed)
Abstract：
Ubiquitin-specific peptidase 16 (USP16) is a deubiquitinase that plays a role in the regulation of gene expression, cell cycle progression, and various other functions. It was originally identified as the major deubiquitinase for histone H2A and has since been found to deubiquitinate a range of other substrates, including proteins from both the cytoplasm and nucleus. USP16 is phosphorylated when cells enter mitosis and dephosphorylated during the metaphase/anaphase transition. While much of USP16 is localized in the cytoplasm, separating the enzyme from its substrates is considered an important regulatory mechanism. Some of the functions that USP16 has been linked to include DNA damage repair, immune disease, tumorigenesis, protein synthesis, coronary artery health, and male infertility. The strong connection to immune response and the fact that multiple oncogene products are substrates of USP16 suggests that USP16 may be a potential therapeutic target for the treatment of certain human diseases.
摘要：
泛素特异性肽酶16（USP16）是一种去泛素酶，在基因表达的调节中起作用，细胞周期进程，以及其他各种功能。它最初被确定为组蛋白H2A的主要去泛素酶，并且此后被发现可使一系列其他底物去泛素，包括来自细胞质和细胞核的蛋白质。USP16在细胞进入有丝分裂时被磷酸化,并且在中期/后期过渡期间被去磷酸化。虽然USP16的大部分位于细胞质中，将酶与其底物分离被认为是重要的调节机制。USP16与DNA损伤修复相关的一些功能，免疫性疾病，肿瘤发生，蛋白质合成，冠状动脉健康，和男性不育。与免疫应答的紧密联系以及多种癌基因产物是USP16的底物的事实表明USP16可能是治疗某些人类疾病的潜在治疗靶标。
