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.
Wenyi Wei, William G. Kaelin Jr.
Title and authors | Publication | Year |
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The Ubiquitin Ligase COP1 Promotes Glioma Cell Proliferation by Preferentially Downregulating Tumor Suppressor p53
S Zou, Y Zhu, B Wang, F Qian, X Zhang, L Wang, C Fu, H Bao, M Xie, S Gao, R Yu, H Shi |
Molecular Neurobiology | 2016 |
High expression of constitutive photomorphogenic 1 (COP1) is associated with poor prognosis in bladder cancer
J Li, L Wang, R Xiao, Q Pan, H Huang, R Kuang |
Tumor Biology | 2016 |
HuCOP1 contributes to the regulation of DNA repair in keratinocytes.
Fazekas B, Carty MP, Németh I, Kemény L, Széll M, Ádám É |
Molecular and Cellular Biochemistry | 2016 |