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DNA damage-related ubiquitinations: One E1 that rules them all

机译：DNA损伤相关的泛素化：一个E1统治着它们

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摘要

Ubiquitin (Ub) and its covalent attachment to proteins (ubiquitination) play a central role in many key processes within a eukaryotic cell. Ubiquitination is a hierarchical three-step process involving activation, conjugation and liga-tion by E1-Ub-activating, E2-Ub-conjugating and E3-Ub-ligating enzymes (E3 ligases), respectively. The biological outcome of ubiquitin ligation to a protein is dictated by the fashion in which the ubiqutin chain is assembled. While a chain of at least four ubiquitin monomers linked by Lys48 or Lys11 leads to protein degradation by the 26S proteasome, the presence of either monoubiquitination or chains linked by Lys63 has been implicated in multiple non-proteolytic processes, including DNA repair. Specificity of the ubiquitination-driven processes is also ensured by a set of substrate-specific E3 ubiquitin ligases that attach the ubiquitin chain to specific targets. This is also the case for DNA damage response (DDR), where E3 ligases, including BRCA1, RNF8, HERC2 and RNF168, cooperate to ubiquitylate numerous proteins at sites of DNA double-strand breaks (DSBs), thereby orchestrating subsequent signaling and repair.
机译：泛素（Ubiquitin，Ub）及其与蛋白质的共价结合（泛素化）在真核细胞的许多关键过程中起着核心作用。泛素化是一个分三步的过程，涉及分别通过E1-Ub激活，E2-Ub结合和E3-Ub连接酶（E3连接酶）进行激活，结合和连接。泛素连接至蛋白质的生物学结果取决于组装泛素链的方式。虽然由Lys48或Lys11连接的至少四个泛素单体链导致26S蛋白酶体降解蛋白质，但是单泛素化或由Lys63连接的链的存在与多种非蛋白水解过程有关，包括DNA修复。泛素驱动过程的特异性也通过一组将泛素链连接到特定靶标的底物特异性E3泛素连接酶来确保。 DNA损伤反应（DDR）也是这种情况，其中E3连接酶（包括BRCA1，RNF8，HERC2和RNF168）协同作用，在DNA双链断裂（DSB）的位点泛化许多蛋白质，从而协调后续的信号传导和修复。

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