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The ubiquitin proteasome pathway (UPP) plays a central role in cellular homeostasis in the processing and degradation of proteins, including those that regulate cell-cycle progression, apoptosis, and DNA repair.1,2 The 26S proteasome, a key element of the UPP, is formed by the 20S proteolytic core and 19S regulatory particle.1-4 Polyubiquitinated proteins that are destined for degradation by the UPP are recognized by the 19S particle and directed to the 20S core, where proteolytic cleavage is mediated by 3 β subunits: β1 (caspase-like activity), β2 (trypsin-like activity), and β5 (chymotrypsin-like activity).1-3,5
Inhibition of proteasome activity may result in growth arrest and cell death due to the accumulation of regulatory proteins and the induction of apoptotic signaling within the cell.1,2