Ubiquitination is a post-translational modification crucial for cellular signaling. A diverse range of enzymes constitute the machinery that mediates attachment of ubiquitin onto target proteins. This diversity allows the targeting of various proteins in a highly regulated fashion. Many of the enzymes have multiple domains or subunits that bind allosteric effectors and exhibit large conformational rearrangements to facilitate regulation. Here we consider recent examples of ubiquitin itself as an allosteric effector of RING and RBR E3 ligases, as well as advances in the understanding of allosteric regulatory elements within HECT E3 ligases.

中文翻译：

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泛素化机制的变构调节模式。


泛素化是一种对细胞信号转导至关重要的翻译后修饰。多种酶构成了介导泛素附着到靶蛋白上的机制。这种多样性允许以高度调控的方式靶向各种蛋白质。许多酶具有多个结构域或亚基，可结合变构效应子并表现出大的构象重排以促进调节。在这里，我们考虑泛素本身作为 RING 和 RBR E3 连接酶的变构效应子的最新例子，以及对 HECT E3 连接酶内变构调节元件的理解的进展。