Structural basis for the linkage specificity of ubiquitin-binding domain and deubiquitinase
Structural basis for the linkage specificity of ubiquitin-binding domain and deubiquitinase
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泛素结合域和去泛素酶连接特异性的结构基础
DOI：
10.1093/jb/mvac031
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发表时间：
2022
期刊：
影响因子：
--
通讯作者：
Sato Yusuke
中科院分区：
文献类型：
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作者：
河野慎吾;白潔;指田吾郎;古河いまり;吉信公美子;北元優梨;高橋智;要匡;荒木喜美;荒木正健;北島智也;Sato Yusuke
泛素化是一种翻译后修饰系统，对调节真核生物的多种生物过程至关重要。泛素（Ub）本身经历翻译后修饰，包括泛素化。Ub的所有7个赖氨酸残基和1个n端氨基都可以作为进一步泛素化的受体，产生8种类型的Ub链。不同连锁类型的Ub链具有不同的细胞功能，被称为“泛素密码”。含有链接特异性Ub结合域（UBDs）的解码分子识别Ub链来调节不同的细胞功能。另一方面，去泛素酶（DUBs）切割Ub链来逆转泛素信号。本文综述了结构研究揭示的UBDs和DUBs对Ub链的连锁特异性识别的分子机制。
Ubiquitination is a post-translational modification system essential for regulating a wide variety of biological processes in eukaryotes. Ubiquitin (Ub) itself undergoes post-translational modifications, including ubiquitination. All seven lysine residues and one N-terminal amino group of Ub can act as acceptors for further ubiquitination, producing eight types of Ub chains. Ub chains of different linkage types have different cellular functions and are referred to as the ‘ubiquitin code’. Decoder molecules that contain linkage-specific Ub-binding domains (UBDs) recognize the Ub chains to regulate different cellular functions. On the other hand, deubiquitinases (DUBs) cleave Ub chains to reverse ubiquitin signals. This review discusses the molecular mechanisms of linkage-specific recognitions of Ub chains by UBDs and DUBs, which have been revealed by structural studies.