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Chinese University of Science and Technology Nature Sub-Journal: Molecular mechanism of E3 ubiquitin ligase recognition of carboxy-terminal arginine-degron

 Last Update: 2022-01-25
 Source: Internet
 Author: User

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Higher eukaryotic cells remove unwanted or misfolded proteins by degradation to maintain the normal level and function of intracellular protein molecules, mainly through the ubiquitin-dependent proteasome system ( UPS )
.

In the UPS pathway, ubiquitin-activating enzyme E1 , ubiquitin-conjugating enzyme E2 , and ubiquitin-ligase E3 cooperate to catalyze the ubiquitin cascade, which modifies substrates and promotes their degradation

Fig.

1 FEM1C and FEM1B selectively recognize different Arg/C-degron

Xu Chao 's research group carried out research on the receptor proteins FEM1 family members FEM1A , FEM1B and FEM1C in the Cul2 E3 ligase complex .

First, through binding experiments, it was found that FEM1 proteins recognize carboxyl arginine C-degron (

Fig.

2 A model of the Cul2 ^FEM1 E3 complex recognizing Arg/C-degron through the receptor protein FEM1 to regulate substrate stability

In this study, nine complex crystal structures of FEM1B or FEM1C and C-degron were analyzed, revealing the molecular mechanism by which Cul2 FEM1 recognizes different Arg/C- ^degronthrough receptor FEM1 family members , and also identified based on the substrate recognition mechanism of FEM1 More potential new substrates of Cul2 FEM1 were identified, and it provided ^{a structural basis}for designing PROTAC -type small molecules targeting Cul2 ^{FEM1 in the future}.

Related papers have been accepted by Nature Chemical Biology and published online on January 4 , 2021 .

Chen Xinyan, a doctoral student in Professor Xu Chao's research group, Liao Shanhui, a special associate researcher, and Yaara Makaros from Itay Koren 's research group are the co-first authors of the paper .

Prof.
Chao Xu and Prof.
Itay Koren are the co-corresponding authors .

Paper link: https://(Ministry of Life Science and Medicine, Hefei National Research Center for Microscale Matter Science, Research Department)

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