Short-lived proteins control gene expression in cells to carry out a number of vital tasks, from helping the brain form connections to helping the body mount an immune defense. These proteins are made in the nucleus and are quickly destroyed once they've done their job.
Despite their importance, the process by which these proteins get broken down and removed from cells once they are no longer needed has eluded scientists for decades—until now.
"The mechanism we found is very simple and quite elegant," added co-lead author Christopher Nardone, a Ph.D. candidate in genetics at HMS."It is a basic science discovery, but there are many implications for the future."It is well established that cells can break down proteins by tagging them with a small molecule called ubiquitin. The tag tells the proteasome that the proteins are no longer needed, and it destroys them.
"What struck me in the beginning is that these proteins are extremely unstable and they have a very short half-life—once they are produced, they carry out their function, and they are quickly degraded afterwards," Gu said. "Once we identified all these proteins, there were many puzzling questions about how the midnolin mechanism actually works," Nardone said.
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