A paper in Cell describes how CBP acetylates type 1 interferon receptors, which eventually leads to antiviral or tumor-suppressing genes being turned on.

Acetylation plays a central role in cytokine receptor signal transduction,  according to a team of led by The Warren Alpert Medical School of Brown University. Signal transduction is a biochemical process inside cells that controls the activity of antiviral and tumor-suppressing genes

“This is a major discovery in the field of signal transduction,” says Eugene Chin, M.D., a research professor at The Warren Alpert Medical School of Brown University  bms.brown.edu and a staff researcher at Rhode Island Hospital. “Tyrosine phosphorylation has so far been considered the major player in signal transduction. But what we discovered challenges this concept.”

In the study, investigators examined how type 1 interferon binds to IFN-a receptor on the cell surface to trigger an immune response.

The researchers found that type 1 interferon receptors call up cytoplasmic CREB-binding protein (CBP) to move up to the cell surface and that CBP acetylates these receptors. This acetylation sparks a cascade that attracts more proteins to create a complex called ISGF3, report the team. Once that occurs, the complex travels to the cell nucleus to switch on antiviral or tumor-suppressing genes.

The paper describing this work will be reported in the October 5 issue of Cell.

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