Harnessing the ubiquitin code to respond to environmental cues.
Harnessing the ubiquitin code to respond to environmental cues.
复制标题
DOI：
10.1042/ebc20210094
复制
发表时间：
2022-08-05
影响因子：
6.4
通讯作者：
中科院分区：
文献类型：
--
作者：
泛素化是一种重要的翻译后信号，使细胞能够适应和响应环境刺激。底物修饰的范围从单个泛素分子到复杂的多聚泛素链，其中不同的链拓扑结构构成了用于修饰许多细胞信号传导途径中蛋白质功能的密码。通过将泛素的C-末端连接到7个赖氨酸残基之一或前一个泛素的N-末端甲硫氨酸1残基来产生不同的泛素链拓扑结构。大量E2结合酶和E3连接酶之间的协同作用不仅支持同型泛素链的形成，而且支持异型混合链或支链的形成。这种复杂的链拓扑结构阵列被含有连接特异性泛素结合结构域的蛋白质识别，并调节许多细胞途径。虽然植物中泛素密码子的许多功能仍然未知，但最近的工作表明，特定的链拓扑结构与特定的分子过程有关。破译泛素密码以及植物如何利用它来科普不断变化的环境对于理解支撑无数胁迫反应和建立环境耐受性的调节机制至关重要。
Ubiquitination is an essential post-translational signal that allows cells to adapt and respond to environmental stimuli. Substrate modifications range from a single ubiquitin molecule to complex polyubiquitin chains, where diverse chain topologies constitute a code that is utilized to modify the functions of proteins in numerous cellular signalling pathways. Diverse ubiquitin chain topologies are generated by linking the C-terminus of ubiquitin to one of seven lysine residues or the N-terminal methionine 1 residue of the preceding ubiquitin. Cooperative action between a large array of E2 conjugating and E3 ligase enzymes supports the formation of not only homotypic ubiquitin chains but also heterotypic mixed or branched chains. This complex array of chain topologies is recognized by proteins containing linkage-specific ubiquitin-binding domains and regulates numerous cellular pathways. Although many functions of the ubiquitin code in plants remain unknown, recent work suggests that specific chain topologies are associated with particular molecular processes. Deciphering the ubiquitin code and how plants utilize it to cope with the changing environment is essential to understand the regulatory mechanisms that underpin myriad stress responses and establishment of environmental tolerance.