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.
In a cross-departmental collaboration, researchers from Harvard Medical School identified a protein called midnolin that plays a key role in degrading many short-lived nuclear proteins. The study shows that midnolin does so by directly grabbing the proteins and pulling them into the cellular waste-disposal system, called the proteasome, where they are destroyed.
The findings are published Aug. 24 in Science.
“These particular short-lived proteins have been known for over 40 years, but no one had established how they are actually degraded,” said co-lead author Xin Gu, a research fellow in neurobiology at HMS.
2023-08-24 16:00:04
Link from phys.org rnrn
