Novel way of modulating SETDB1 activity


There are many types of cancers in humans. These diseases are caused by abnormal cell growth. Cancer cells have the potential to spread to other parts of the body. Scientists have already identified a lot of risk factors for cancer, such as obesity, smoking, unhealthy diet, consumption of alcohol, and lack of physical exercises. Furthermore, genetic factors also play a central role in cancer development. Based on this information, scientists are searching for ways to combat cancer.

In an article published in Molecular Cell, Moffitt Cancer Center scientists report a novel method, which involves monoubiquitination, to modulate the activity of the SETDB1 protein. SETDB1, which is an enzyme, can be upregulated in many cancer types.

Ubiquitination is a kind of protein modification, regulating a range of critical cellular activities. The addition of ubiquitin to a substrate protein is called ubiquitination. This generally involves three enzymes, known as E1, E2, E3. Ubiquitin is a small regulatory protein that exists widely in our cells. Monoubiquitination, which means the addition of a single ubiquitin protein, may result in activating of protein signaling pathways, or target other proteins for ubiquitination.

The protein SETDB1 is implicated in DNA compaction and modulates gene expression. Active SETDB1 can suppress the expression of certain genes. So it's essential to carefully control SETDB1 activity to maintain normal cellular activities.

The research team found that the SETDB1 protein is bound to a single ubiquitin protein. This modification renders its activity and thus the expression of target genes is inhibited. Two enzymes, E1 and E2, are involved in the monoubiquitination process, while the E3 enzyme does not participate. According to Jia Fang, who led the study, the E2 enzyme could serve as a potential target for cancer treatment.
 
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