Ubiquitin plays a crucial role in cellular processes by regulating protein stability, but USP28 inhibitors, aimed at inhibiting cancer growth, also affect USP25, causing significant side effects. Researchers at the University of Würzburg discovered why USP28 and USP25 inhibitors are non-specific and are now working on developing more precise inhibitors.
Ubiquitin, a small protein, plays a crucial role in nearly every cellular process by regulating the stability and function of most proteins. When ubiquitin attaches to other proteins, it typically marks them for degradation. However, this process can be reversed by specific enzymes. One such enzyme, USP28, helps stabilize proteins that are essential for cell growth and division, which can also contribute to the development of cancer.
The structure of USP28 in complex with the inhibitor AZ1. All amino acids that are similar or identical to USP25 are highlighted. In particular, the region where the inhibitor binds is identical in both proteins. Credit: Kisker/JMU
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