Proteasome endopeptidase complex

The proteasome endopeptidase complex is a large, multi-subunit protease complex essential for intracellular protein degradation. It exists primarily in the 26S and 20S forms: the 20S core is composed of four stacked rings (each with seven subunits), which form a central proteolytic chamber capable of cleaving peptide bonds with broad specificity. Protein substrates are typically recognized following polyubiquitination, unfolded, and translocated into the catalytic core for degradation into peptides. This process is fundamental for protein quality control, regulation of the cell cycle, response to cellular stress, and antigen processing for immune surveillance. Clinically, the proteasome is an important anticancer target, particularly in hematological malignancies such as multiple myeloma, where inhibitors disrupt the degradation of proapoptotic factors and key regulators, resulting in cell cycle arrest and cell death

Other names

ingensinmacropainmulticatalytic endopeptidase complexprosomemulticatalytic proteinase complexMCPproteasomelarge multicatalytic proteaseproteasome organellealkaline protease26S proteasetricorn proteinasetricorn protease

Inhibition of proteolytic activity (especially chymotrypsin-like activity of the 20S subunit), Blocking the degradation of ubiquitinated proteins, Inducing apoptosis in target cells