卡林
泛素
泛素蛋白连接酶类
泛素连接酶
细胞生物学
蛋白酶体
生物
蛋白质降解
计算机科学
生物化学
计算生物学
化学
基因
作者
Henry C. Nguyen,Wei Wang,Yong Xiong
出处
期刊:Sub-cellular biochemistry
日期:2017-01-01
卷期号:: 323-347
被引量:41
标识
DOI:10.1007/978-3-319-46503-6_12
摘要
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.
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