Structural highlights
Function
FEM1C_HUMAN Probable component of an E3 ubiquitin-protein ligase complex, in which it may act as a substrate recognition subunit.
Publication Abstract from PubMed
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.
Molecular basis for ubiquitin ligase CRL2(FEM1C)-mediated recognition of C-degron.,Yan X, Wang X, Li Y, Zhou M, Li Y, Song L, Mi W, Min J, Dong C Nat Chem Biol. 2021 Jan 4. pii: 10.1038/s41589-020-00703-4. doi:, 10.1038/s41589-020-00703-4. PMID:33398170[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Yan X, Wang X, Li Y, Zhou M, Li Y, Song L, Mi W, Min J, Dong C. Molecular basis for ubiquitin ligase CRL2(FEM1C)-mediated recognition of C-degron. Nat Chem Biol. 2021 Jan 4. pii: 10.1038/s41589-020-00703-4. doi:, 10.1038/s41589-020-00703-4. PMID:33398170 doi:http://dx.doi.org/10.1038/s41589-020-00703-4
