End-Binding E3 Ubiquitin Ligases Enable Protease Signaling,ACS Chemical Biology

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End-Binding E3 Ubiquitin Ligases Enable Protease Signaling
ACS Chemical Biology ( IF 3.5 ) Pub Date : 2019-11-12 , DOI: 10.1021/acschembio.9b00621
Matthew Ravalin ₁ , Koli Basu ₁ , Jason E Gestwicki _{1,

2} , Charles S Craik ₁

Affiliation

Post-translational modifications (PTMs) direct the assembly of protein complexes. In this context, proteolysis is a unique PTM because it is irreversible; the hydrolysis of the peptide backbone generates separate fragments bearing a new N and C terminus. Proteolysis can “re-wire” protein–protein interactions (PPIs) via the recruitment of end-binding proteins to new termini. In this review, we focus on the role of proteolysis in specifically creating complexes by recruiting E3 ubiquitin ligases to new N and C termini. These complexes potentiate proteolytic signaling by “erasing” proteolytic modifications. This activity tunes the duration and magnitude of protease signaling events. Recent work has shown that the stepwise process of proteolysis, end-binding by E3 ubiquitin ligases, and fragment turnover is associated with both the nascent N terminus (i.e., N-degron pathways) and the nascent C terminus (i.e., the C-degron pathways). Here, we discuss how these pathways might harmonize protease signaling with protein homeostasis (i.e., proteostasis).

中文翻译：

末端结合 E3 泛素连接可实现蛋白酶信号传导

翻译后修饰 (PTM) 指导蛋白质复合物的组装。在这种情况下，蛋白水解是一种独特的 PTM，因为它是不可逆的。肽主链的水解产生带有新 N 和 C 末端的单独片段。蛋白水解可以通过将末端结合蛋白招募到新末端来“重新连接”蛋白质-蛋白质相互作用（PPI）。在这篇综述中，我们重点关注蛋白水解在通过将 E3 泛素连接酶招募到新的 N 和 C 末端来特异性创建复合物中的作用。这些复合物通过“消除”蛋白水解修饰来增强蛋白水解信号传导。该活性调节蛋白酶信号事件的持续时间和强度。最近的工作表明，蛋白水解、E3 泛素连接酶末端结合和片段周转的逐步过程与新生 N 末端（即 N-降解决定子途径）和新生 C 末端（即 C-降解决定子途径）相关。途径）。在这里，我们讨论这些途径如何协调蛋白酶信号传导与蛋白质稳态（即蛋白质稳态）。

更新日期：2019-11-12

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