Cullin-RING E3 Ubiquitin Ligases: Bridges to Destruction.
Cullin-RING E3 Ubiquitin Ligases: Bridges to Destruction.
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DOI：
10.1007/978-3-319-46503-6_12
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发表时间：
2017
影响因子：
--
通讯作者：
Xiong Y
中科院分区：
文献类型：
--
作者：
Nguyen HC;Wang W;Xiong Y
泛素化是真核生物中高度保守的翻译后修饰，以靶向蛋白质被 26S 蛋白酶体降解而闻名。 E3 泛素连接酶选择用于蛋白酶体降解的蛋白质。 Cullin-RING E3 泛素连接酶 (CRL) 是最大的 E3 泛素连接酶超家族，在哺乳动物中已知有 400 多个成员。这些模块复合物在细胞中受到严格调控。在本章中，我们重点介绍了最近的结构和生化进展，揭示了 cullin-RING 连接酶的组装和结构、各种宿主因素的动态调节以及病毒病原体和小分子对它们的操纵。
Ubiquitination is a highly conserved post-translational modification in eukaryotes, well known for targeting proteins for degradation by the 26S proteasome. Proteins destined for proteasomal degradation are selected by E3 ubiquitin ligases. Cullin-RING E3 ubiquitin ligases (CRLs) are the largest superfamily of E3 ubiquitin ligases, with over 400 members known in mammals. These modular complexes are tightly regulated in the cell. In this chapter, we highlight recent structural and biochemical advances shedding light on the assembly and architecture of cullin- RING ligases, their dynamic regulation by a variety of host factors, and their manipulation by viral pathogens and small molecules.