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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.
Authors
Wenyi Wei, William G. Kaelin Jr.
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Citation information
Citations to this article in year 2015 (4)
| Title and authors | Publication | Year |
|---|---|---|
|
COP1 enhances ubiquitin-mediated degradation of p27Kip1 to promote cancer cell growth
HH Choi, L Phan, PC Chou, CH Su, SC Yeung, JS Chen, MH Lee |
Oncotarget | 2015 |
|
Regulating the stability and localization of CDK inhibitor p27 Kip1 via CSN6-COP1 axis
HH Choi, S Guma, L Fang, L Phan, C Ivan, K Baggerly, A Sood, MH Lee |
Cell cycle (Georgetown, Tex.) | 2015 |
|
COP1, the negative regulator of ETV1, influences prognosis in triple-negative breast cancer
M Ouyang, H Wang, J Ma, W Lü, J Li, C Yao, G Chang, J Bi, S Wang, W Wang |
BMC Cancer | 2015 |
|
CSN6 deregulation impairs genome integrity in a COP1-dependent pathway
Choi HH, Su CH, Fang L, Zhang J, Yeung SC, Lee MH |
Oncotarget | 2015 |
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