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Mechanisms of Deubiquitinase Specificity and Regulation
Annual Review of Biochemistry ( IF 12.1 ) Pub Date : 2017-06-27 00:00:00 , DOI: 10.1146/annurev-biochem-061516-044916
Tycho E T Mevissen 1 , David Komander 1
Affiliation  

Protein ubiquitination is one of the most powerful posttranslational modifications of proteins, as it regulates a plethora of cellular processes in distinct manners. Simple monoubiquitination events coexist with more complex forms of polyubiquitination, the latter featuring many different chain architectures. Ubiquitin can be subjected to further posttranslational modifications (e.g., phosphorylation and acetylation) and can also be part of mixed polymers with ubiquitin-like modifiers such as SUMO (small ubiquitin-related modifier) or NEDD8 (neural precursor cell expressed, developmentally downregulated 8). Together, cellular ubiquitination events form a sophisticated and versatile ubiquitin code. Deubiquitinases (DUBs) reverse ubiquitin signals with equally high sophistication. In this review, we conceptualize the many layers of specificity that DUBs encompass to control the ubiquitin code and discuss examples in which DUB specificity has been understood at the molecular level. We further discuss the many mechanisms of DUB regulation with a focus on those that modulate catalytic activity. Our review provides a framework to tackle lingering questions in DUB biology.

中文翻译:


去泛素酶特异性和调控机制

蛋白质泛素化是蛋白质最强大的翻译后修饰之一,因为它以不同的方式调节过多的细胞过程。简单的单泛素化事件与更复杂的多泛素化形式共存,后者具有许多不同的链结构。泛素可以进行进一步的翻译后修饰(例如,磷酸化和乙酰化),也可以是具有泛素样修饰剂的混合聚合物的一部分,例如 SUMO(小泛素相关修饰剂)或 NEDD8(神经前体细胞表达,发育下调 8) . 一起,细胞泛素化事件形成了一个复杂而通用的泛素代码。去泛素酶 (DUB) 以同样高的复杂性逆转泛素信号。在本次审查中,我们将 DUB 包含的多层特异性概念化以控制泛素代码,并讨论在分子水平上理解 DUB 特异性的示例。我们进一步讨论了 DUB 调节的许多机制,重点是那些调节催化活性的机制。我们的审查提供了一个框架来解决 DUB 生物学中挥之不去的问题。

更新日期:2017-06-27
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