In eukaryotic cells, proteome remodeling is mediated by the ubiquitin-proteasome system, which regulates protein degradation, trafficking, and signaling events in the cell. Interplay between the cellular proteome and ubiquitin is complex and dynamic and many regulatory features that support this system have only recently come into focus. An unexpected recurring feature in this system is the physical interaction between E3 ubiquitin ligases and deubiquitylases (DUBs). Recent studies have reported on the regulatory significance of DUB-E3 interactions and it is becoming clear that they play important but complicated roles in the regulation of diverse cellular processes. Here, we summarize the current understanding of interactions between ubiquitin conjugation and deconjugation machineries and we examine the regulatory logic of these enigmatic complexes.

中文翻译：

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结合共轭和去共轭活动，以实现细胞泛素动力学。

在真核细胞中，蛋白质组重塑由泛素-蛋白酶体系统介导，该系统调节细胞中的蛋白质降解，运输和信号传导事件。细胞蛋白质组和泛素之间的相互作用是复杂而动态的，支持该系统的许多调节功能直到最近才成为人们关注的焦点。该系统中意外的重复特征是E3泛素连接酶和去泛素酶（DUB）之间的物理相互作用。最近的研究已经报道了DUB-E3相互作用的调节意义，并且越来越清楚的是，它们在多种细胞过程的调节中起着重要而复杂的作用。这里，