PSMA1 Human

The proteasome is a multicatalytic proteinase complex with a highly ordered 20S core structure. This core structure is composed of four rings of 28 non-identical subunits: two rings are composed of seven alpha subunits, and two rings are composed of seven beta subunits . The alpha subunits, including PSMA1, form the outer rings of the proteasome and act as a gate for substrate entry into the proteolytic chamber .

The primary function of the proteasome is to degrade unneeded or damaged proteins by proteolysis, a chemical reaction that breaks peptide bonds . This process is ATP/ubiquitin-dependent and occurs in a non-lysosomal pathway . The proteasome is essential for various cellular processes, including the regulation of the cell cycle, modulation of various signaling pathways, and the removal of misfolded proteins .

Mutations or dysregulation of the PSMA1 gene have been associated with several diseases, including cystic fibrosis and Parkinson’s disease . The proteasome’s role in degrading misfolded proteins is particularly relevant in neurodegenerative diseases, where the accumulation of such proteins can lead to cellular dysfunction and death .

Recombinant PSMA1 is produced using recombinant DNA technology, which involves inserting the PSMA1 gene into an expression system to produce the protein in a controlled environment. This recombinant protein is used in various research applications to study the structure and function of the proteasome, as well as its role in disease .

Research on PSMA1 and the proteasome complex has significant implications for understanding cellular homeostasis and developing therapeutic strategies for diseases related to protein degradation. Inhibitors of the proteasome, such as bortezomib, are already used in the treatment of multiple myeloma and other cancers .