Coordinated Actions Between p97 and Cullin-RING Ubiquitin Ligases for Protein Degradation.
Coordinated Actions Between p97 and Cullin-RING Ubiquitin Ligases for Protein Degradation.
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DOI：
10.1007/978-981-15-1025-0_5
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发表时间：
2020
影响因子：
--
通讯作者：
Wenbo Shi;Ran Ding;Pei Zhou;Yuan Fang;Ruixi Wan;Yilin Chen;Jianping Jin
中科院分区：
文献类型：
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作者：
Wenbo Shi;Ran Ding;Pei Zhou;Yuan Fang;Ruixi Wan;Yilin Chen;Jianping Jin
cullin-RING泛素连接酶是泛素连接酶中最大的亚家族。它们控制真核生物中大量蛋白质底物的泛素化和降解。p97是一种含有ATP酶结构域的蛋白分离酶。它在泛素-蛋白酶体途径中的后泛素化事件中起重要作用。p97与其辅因子一起与泛素连接酶合作，提取泛素化底物并将其递送至蛋白酶体进行蛋白水解。本文综述了p97与其辅因子和Cullin-RING泛素连接酶在细胞蛋白质降解中的结构、功能和机制。
The cullin-RING ubiquitin ligases comprise the largest subfamily of ubiquitin ligases. They control ubiquitylation and degradation of a large number of protein substrates in eukaryotes. p97 is an ATPase domain-containing protein segregase. It plays essential roles in post-ubiquitylational events in the ubiquitin-proteasome pathway. Together with its cofactors, p97 collaborates with ubiquitin ligases to extract ubiquitylated substrates and deliver them to the proteasome for proteolysis. Here we review the structure, functions, and mechanisms of p97 in cellular protein degradation in coordination with its cofactors and the cullin-RING ubiquitin ligases.