Department of Biochemistry and Biophysics, UNC Chapel Hill School of Medicine, Chapel Hill, NC 27599, U.S.A.
Department of Pharmacology and Lineberger Comprehensive Care Center, UNC Chapel Hill School of Medicine, Chapel Hill, NC 27599, U.S.A.
Biochem Soc Trans. 2024 Feb 28;52(1):241-267. doi: 10.1042/BST20230454.
Protein ubiquitination is a post-translational modification that entails the covalent attachment of the small protein ubiquitin (Ub), which acts as a signal to direct protein stability, localization, or interactions. The Ub code is written by a family of enzymes called E3 Ub ligases (∼600 members in humans), which can catalyze the transfer of either a single ubiquitin or the formation of a diverse array of polyubiquitin chains. This code can be edited or erased by a different set of enzymes termed deubiquitinases (DUBs; ∼100 members in humans). While enzymes from these distinct families have seemingly opposing activities, certain E3-DUB pairings can also synergize to regulate vital cellular processes like gene expression, autophagy, innate immunity, and cell proliferation. In this review, we highlight recent studies describing Ub ligase-DUB interactions and focus on their relationships.
蛋白质泛素化是一种翻译后修饰，涉及到将小蛋白泛素（Ub）共价连接，Ub 作为一种信号，可直接影响蛋白质的稳定性、定位或相互作用。Ub 密码由一组称为 E3 泛素连接酶（人类约有 600 个成员）的酶家族编写，这些酶可以催化单个泛素的转移或多种泛素链的形成。这一密码可以通过另一组称为去泛素化酶（DUB；人类约有 100 个成员）的酶来编辑或擦除。尽管来自这些不同家族的酶具有看似相反的活性，但某些 E3-DUB 配对也可以协同调节重要的细胞过程，如基因表达、自噬、先天免疫和细胞增殖。在这篇综述中，我们强调了最近描述泛素连接酶-DUB 相互作用的研究，并重点介绍了它们之间的关系。
