Deubiquitinating enzymes (DUBs) are proteins that can remove a small protein called ubiquitin from other proteins. This can change how stable and functional those proteins are.
Researchers from FORMA Therapeutics have compared two related DUBs, USP25 and USP28, which have similar overall structures but different functions in the cell. USP28 stabilises certain proteins in the nucleus, while USP25 regulates signaling pathways involved in inflammation.
The team collected diffraction data from multiple beamlines at Diamond, and the ESRF, and analysed SAXS (SEC) data from Diamond's beamline B21 to determine the size and shape of the proteins and their oligomerisation state (by mass).
This study helps to understand how DUBs can regulate different processes in the cell through their oligomerisation state and activity. The results will provide a better understanding of how these proteins function in the body and how they may be targeted for therapeutic purposes; for example, in the treatment of certain types of cancer and inflammatory diseases with which these proteins have been associated.
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