The Pleiotropic Ubiquitin-Specific Peptidase 16 and Its Many Substrates.

The Pleiotropic Ubiquitin-Specific Peptidase 16 and Its Many Substrates.
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DOI:
10.3390/cells12060886
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发表时间:
2023-03-13
期刊:
影响因子:
6
通讯作者:
--
中科院分区:
生物学2区
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泛素特异性肽酶16(USP 16)是一种去泛素化酶,在基因表达、细胞周期进程和各种其他功能的调节中发挥作用。它最初被鉴定为组蛋白H2 A的主要去泛素化酶,并且已经发现去泛素化一系列其他底物,包括来自细胞质和细胞核的蛋白质。当细胞进入有丝分裂时,USP 16被磷酸化,并在中期/后期转换期间去磷酸化。虽然USP 16的大部分位于细胞质中,但将酶与其底物分离被认为是一种重要的调节机制。USP 16与DNA损伤修复、免疫疾病、肿瘤发生、蛋白质合成、冠状动脉健康和男性不育有关。与免疫反应的密切联系以及多种癌基因产物是USP 16底物的事实表明,USP 16可能是治疗某些人类疾病的潜在治疗靶点。
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.
USP16通过CDKN2A调节调节原代组织中的Wnt信号传导。
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