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-related enzymes USP28 and USP25 play critical roles in cell processes, but their similar structures lead to challenges in cancer treatment with current inhibitors.
Research at the University of Würzburg aims to refine these inhibitors to target more specifically and reduce side effects. 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. In order to reduce the stability of these proteins and thus inhibit cancer growth, inhibitors of USP28 have been developed.
These inhibitors, which form the basis of many anti-cancer drugs currently in development, disrupt cell division by blocking the USP28 enzyme. The problem is that they often act not only against USP28 but also against USP25, a closely related enzyme that separates ubiquitin from .