Good COP1 or bad COP1? In vivo veritas.
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- Record sourced from PubMed, PMID 21403396.
- Also identified by DOI 10.1172/JCI57080 and PMC identifier 3069793.
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Abstract
The evolutionarily conserved protein COP1 has been shown to operate as an E3 ubiquitin ligase complex, and a number of putative substrates have been identified, including the c-JUN oncoprotein and p53 tumor suppressor protein. New work by Migliorini and colleagues described in the current issue of JCI demonstrates that COP1 acts as a tumor suppressor in vivo and does so, at least in part, by promoting the destruction of c-JUN. These findings challenge the view that COP1 regulates p53 stability and call into question the wisdom of developing COP1 inhibitors as potential anticancer agents.
Medical subject headings
- Nuclear Proteins
- Ubiquitin-Protein Ligases