The Multifaceted Roles of USP15 in Signal Transduction.

The Multifaceted Roles of USP15 in Signal Transduction.
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DOI:
10.3390/ijms22094728
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发表时间:
2021-04-29
影响因子:
5.6
通讯作者:
Kim EE
Kim EE
中科院分区:
生物学2区
文献类型:
--
作者:
Das T;Song EJ;Kim EE

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泛素化(Ubiquitination)和去泛素化(deubiquitination)是蛋白质翻译后修饰的过程,在维持泛素稳态、控制蛋白质稳定性和调节多种信号通路等复杂的细胞网络中起着重要的调节作用。因此,一些参与泛素化和去泛素化的酶,特别是E3连接酶和去泛素化酶,已经引起了药物发现的关注。在这里,我们回顾了最近的研究结果USP15,一个去泛素化酶,调节不同的信号通路,通过去泛素化重要的靶蛋白。尽管之前的几项基础研究已经揭示了USP15在不同信号网络中的多功能作用,但这些研究尚未进行系统和具体的综述,这些研究可以提供有关可能的疾病标志物和临床应用的重要信息。本文综述了USP15对不同信号通路的调控机制,其中动态反向泛素化是一个关键的调节器。
Ubiquitination and deubiquitination are protein post-translational modification processes that have been recognized as crucial mediators of many complex cellular networks, including maintaining ubiquitin homeostasis, controlling protein stability, and regulating several signaling pathways. Therefore, some of the enzymes involved in ubiquitination and deubiquitination, particularly E3 ligases and deubiquitinases, have attracted attention for drug discovery. Here, we review recent findings on USP15, one of the deubiquitinases, which regulates diverse signaling pathways by deubiquitinating vital target proteins. Even though several basic previous studies have uncovered the versatile roles of USP15 in different signaling networks, those have not yet been systematically and specifically reviewed, which can provide important information about possible disease markers and clinical applications. This review will provide a comprehensive overview of our current understanding of the regulatory mechanisms of USP15 on different signaling pathways for which dynamic reverse ubiquitination is a key regulator.
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