The 26S proteasome is a multicatalytic proteinase complex with a highly ordered structure composed of two complexes: a 20S core and a 19S regulator . The 20S core is made up of four rings of 28 non-identical subunits, with two rings composed of seven alpha subunits and two rings composed of seven beta subunits . The 19S regulator consists of a base, which contains six ATPase subunits and two non-ATPase subunits, and a lid, which contains up to ten non-ATPase subunits .
PSME3 is a subunit of the 11S regulator, which is an alternate regulator of the proteasome . The 11S regulator, also known as PA28, replaces the 19S regulator in the immunoproteasome, a modified form of the proteasome that processes class I MHC peptides . The gamma subunit of the 11S regulator, encoded by the PSME3 gene, forms a homohexameric ring composed of six gamma subunits .
PSME3 plays a significant role in various cellular processes, including the regulation of the cell cycle, apoptosis, and the immune response . It is involved in the degradation of proteins that are ubiquitinated, a process that tags proteins for degradation by the proteasome . The immunoproteasome, which includes the 11S regulator, is essential for the processing of class I MHC peptides, which are crucial for the immune response .
Recombinant PSME3 is used in various research applications to study its structure, function, and role in disease processes . Understanding the mechanisms by which PSME3 regulates the proteasome and its involvement in cellular processes can provide insights into potential therapeutic targets for diseases associated with proteasome dysfunction .