德隆
泛素
泛素连接酶
细胞生物学
突变
蛋白质降解
DNA连接酶
泛素蛋白连接酶类
化学
蛋白酶体
生物
卡林
生物化学
突变
酶
基因
作者
Xiao‐Jie Yan,Xiaolu Wang,Yao Li,Mengqi Zhou,Yanjun Li,Lili Song,Wenyi Mi,Jinrong Min,Dong Cheng
标识
DOI:10.1038/s41589-020-00703-4
摘要
Proteome integrity depends on the ubiquitin-proteasome system to degrade unwanted or abnormal proteins. In addition to the N-degrons, C-terminal residues of proteins can also serve as degradation signals (C-degrons) that are recognized by specific cullin-RING ubiquitin ligases (CRLs) for proteasomal degradation. FEM1C is a CRL2 substrate receptor that targets the C-terminal arginine degron (Arg/C-degron), but the molecular mechanism of substrate recognition remains largely elusive. Here, we present crystal structures of FEM1C in complex with Arg/C-degron and show that FEM1C utilizes a semi-open binding pocket to capture the C-terminal arginine and that the extreme C-terminal arginine is the major structural determinant in recognition by FEM1C. Together with biochemical and mutagenesis studies, we provide a framework for understanding molecular recognition of the Arg/C-degron by the FEM family of proteins.
科研通智能强力驱动
Strongly Powered by AbleSci AI