| 去泛素化酶PSMD14在肿瘤中的研究进展 |
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| 引用本文： | 段远胜,井超,王旭东.去泛素化酶PSMD14在肿瘤中的研究进展[J].中国肿瘤临床,2022,49(8):407-410. |
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| 作者姓名： | 段远胜 井超 王旭东 |
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| 作者单位： | 天津医科大学肿瘤医院颌面耳鼻喉肿瘤科，国家肿瘤临床医学研究中心，天津市"肿瘤防治"重点实验室，天津市恶性肿瘤临床医学研究中心（天津市300060） |
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| 基金项目： | 本文课题受国家自然科学基金面上项目（编号:82073002）资助 |
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| 摘 要： | 泛素蛋白酶体系统（ubiquitin proteasome system, UPS）能够介导真核细胞中80%以上蛋白质的降解，对底物的蛋白稳定和功能发挥起到关键作用。作为一种重要的泛素化修饰调控因子，去泛素化酶能够从底物上切割泛素，修饰泛素链并加工泛素前体，与多种生理病理过程密切相关。其中，去泛素化酶PSMD14（proteasome 26S subunit，non-ATPase 14）位于蛋白酶体26S亚基，是一种非ATP酶组分。近年来，其在肿瘤发生发展中的作用越来越受到关注。本文将对PSMD14的结构、作用机制及其抑制剂在肿瘤中的研究进展进行综述。
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| 关 键 词： | 去泛素化酶 肿瘤 PSMD14 |
| 收稿时间： | 2021-08-10 |
Research progress on deubiquitinating enzyme PSMD14 in human cancers |
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| Affiliation: | Department of Maxillofacial and Otorhinolaryngological Oncology, Tianjin Medical University Cancer Institute & Hospital, National Clinical Research Center for Cancer, Tianjin Key Laboratory of Cancer Prevention and Therapy, Tianjin’s Clinical Research Center for Cancer, Tianjin 300060, China |
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| Abstract: | The ubiquitin proteasome system (UPS), which mediates the degradation of more than 80% proteins in eukaryotic cells, plays a crucial role in orchestrating the stabilization and function of substrates. As a key regulator of ubiquitination, deubiquitinating enzymes (DUBs) could cleave ubiquitin from the substrates, modify ubiquitin chains and process ubiquitin precursors, which is associated with various physiological and pathological processes. Among these DUBs, proteasome 26S subunit non-ATPase 14 (PSMD14) is a component of proteasome 26S subunit without ATPase activity, whose effects on tumorigenesis and progression are paid more and more attention to. Here, the research progress on the expressions, mechanisms and inhibitors of PSMD14 in human cancers is reviewed in this paper. |
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