Proximity Proteomics Reveals Otud6B Regulation Of Stress Granule Dynamics Through Coalescence With VCP/P97
Our cells are constantly exposed to various stresses, and to cope, they form temporary compartments called stress granules. Think of these as cellular “safe deposit boxes” where important molecules are stored and protected until the stress passes. However, if these stress granules don’t form or disappear properly, it can contribute to diseases like neurodegeneration.
New research has shed light on a key player in this process: an enzyme called OTUD6B. This enzyme was found to be directly involved in how stress granules are put together and taken apart. Specifically, OTUD6B works in conjunction with another protein, VCP/p97, which is already known to be important for breaking down these granules.
The study showed that OTUD6B not only helps stress granules form efficiently but also ensures their timely clearance once the stress is gone. This partnership between OTUD6B and VCP/p97 is crucial for the cell’s ability to respond to and recover from stressful conditions. Understanding how these proteins work together could open new avenues for therapeutic strategies in diseases where stress granule regulation goes awry.
Source: link to paper