期刊
NATURE CHEMICAL BIOLOGY
卷 17, 期 3, 页码 254-+出版社
NATURE PORTFOLIO
DOI: 10.1038/s41589-020-00704-3
关键词
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资金
- `Strategic Priority Research Program' of the Chinese Academy of Sciences [XDB19000000]
- National Natural Science Foundation of China [92053107, 31770806]
- Major/Innovative Program of the Development Foundation of the Hefei Center for Physical Science and Technology [2018CXFX007]
- Thousand Young Talent program
- Alon fellowship for outstanding young researchers
This study reveals the molecular mechanism of Arg/C-degron recognition by FEM1 proteins and demonstrates that FEM1A/C and FEM1B selectively target distinct classes of Arg/C-degrons.
Degrons are elements within protein substrates that mediate the interaction with specific degradation machineries to control proteolysis. Recently, a few classes of C-terminal degrons (C-degrons) that are recognized by dedicated cullin-RING ligases (CRLs) have been identified. Specifically, CRL2 using the related substrate adapters FEM1A/B/C was found to recognize C degrons ending with arginine (Arg/C-degron). Here, we uncover the molecular mechanism of Arg/C-degron recognition by solving a subset of structures of FEM1 proteins in complex with Arg/C-degron-bearing substrates. Our structural research, complemented by binding assays and global protein stability (GPS) analyses, demonstrates that FEM1A/C and FEM1B selectively target distinct classes of Arg/C-degrons. Overall, our study not only sheds light on the molecular mechanism underlying Arg/C-degron recognition for precise control of substrate turnover, but also provides valuable information for development of chemical probes for selectively regulating proteostasis.
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