AI Article Synopsis
- COP1 proteins are crucial E3 ubiquitin ligases that assist in plant phototropism and the degradation of specific transcription factors in mammals.
- The research focuses on the structure of the COP1 WD40 domain, revealing it as a seven-bladed β propeller that interacts with the Trib1 peptide in a way that suggests a common mechanism for peptide recognition by COP1.
- The findings enhance our understanding of how COP1 identifies target motifs and provide insights into the regulation of Trib1 that ultimately leads to the degradation of C/EBPα.
Article Abstract
COP1 proteins are E3 ubiquitin ligases that regulate phototropism in plants and target transcription factors for degradation in mammals. The substrate-binding region of COP1 resides within a WD40-repeat domain that also binds to Trib proteins, which are adaptors for C/EBPα degradation. Here we report structures of the human COP1 WD40 domain in isolation, and complexes of the human and Arabidopsis thaliana COP1 WD40 domains with the binding motif of Trib1. The human and Arabidopsis WD40 domains are seven-bladed β propellers with an inserted loop on the bottom face of the first blade. The Trib1 peptide binds in an extended conformation to a highly conserved surface on the top face of the β propeller, indicating a general mode for recognition of peptide motifs by COP1. Together, these studies identify the structural basis and key interactions for motif recognition by COP1, and hint at how Trib1 autoinhibition is overcome to target C/EBPα for degradation.
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|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4856590 | PMC |
| http://dx.doi.org/10.1016/j.str.2016.03.002 | DOI Listing |
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