We found a match
Your institution may have access to this item. Find your institution then sign in to continue.
- Title
Good COP1 or bad COP1? In vivo veritas.
- Authors
Wenyi Wei; Kaelin Jr., William G.
- 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.
- Subjects
PROTEIN-protein interactions; UBIQUITIN; LIGASES; IMMUNOSUPPRESSION; P53 protein; ANTINEOPLASTIC agents
- Publication
Journal of Clinical Investigation, 2011, Vol 121, Issue 4, p1263
- ISSN
0021-9738
- Publication type
Opinion
- DOI
10.1172/JCI57080