Deubiquitylation of deubiquitylases.

Deubiquitylation of deubiquitylases.
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DOI:
10.1098/rsob.170016
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发表时间:
2017-06
期刊:
影响因子:
5.8
通讯作者:
Ramakrishna S
Ramakrishna S
中科院分区:
生物学2区
文献类型:
--
作者:
Haq S;Ramakrishna S

文献摘要

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去泛素化酶 (DUB) 逆转靶蛋白的泛素化,从而调节多种细胞功能。与针对 DUB 对抗细胞蛋白或自动泛素化 E3 连接酶降解的能力进行的大量研究相比,人们对 DUB 调节机制知之甚少。在这篇综述论文中,我们总结了其他 DUB 去泛素化的一种新的可能机制。现有数据表明需要进一步的实验来验证和描述“配音 DUB”的概念。目前的研究表明,通过其他 DUB 去泛素化的想法仍处于起步阶段。尽管如此,未来的研究有望验证这一概念。
Deubiquitylating enzymes (DUBs) reverse the ubiquitylation of target proteins, thereby regulating diverse cellular functions. In contrast to the plethora of research being conducted on the ability of DUBs to counter the degradation of cellular proteins or auto-ubiquitylated E3 ligases, very little is known about the mechanisms of DUB regulation. In this review paper, we summarize a novel possible mechanism of DUB deubiquitylation by other DUBs. The available data suggest the need for further experiments to validate and characterize this notion of ‘Dubbing DUBs’. The current studies indicate that the idea of deubiquitylation of DUBs by other DUBs is still in its infancy. Nevertheless, future research holds the promise of validation of this concept.