alexa Geminivirus C2 protein might be the key player for geminiviral co- option of SCF-mediated ubiquitination.
Biomedical Sciences

Biomedical Sciences

Journal of Biomedical Systems & Emerging Technologies

Author(s): LozanoDuran R, Bejarano ER

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Abstract Viruses are obligate intracellular parasites, and need to create a suitable cell environment for viral propagation to complete their life cycle. In order to achieve this, viruses must usurp or interfere with the cellular machinery. Ubiquitination, a post-translational modification that controls numerous cellular processes, has proven to be a common target for viruses. Recently, geminivirus C2 protein has been shown to interact with the CSN complex and disrupt its activity over CULLIN1, interfering with the function of the CULLIN1-based SCF ubiquitin E3 ligases. Interestingly, overexpression of a given F-box protein may circumvent the general SCF malfunction caused by C2. This result raises the tantalizing idea that geminiviruses might be not only hampering, but also redirecting the activity of SCF complexes, thus co-opting the SCF-mediated ubiquitination pathway. We hypothesize that the mechanism of C2-facilitated co-option of SCF-mediated ubiquitination might not be exclusive for geminiviruses, but rather a common strategy for viruses.
This article was published in Plant Signal Behav and referenced in Journal of Biomedical Systems & Emerging Technologies

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