Proteasome 26S Subunit, Non-ATPase 5 (PSMD5) is a component of the 26S proteasome, a complex and essential protease machinery in eukaryotic cells. The 26S proteasome is responsible for the ATP-dependent degradation of ubiquitinated proteins, playing a crucial role in maintaining cellular homeostasis by removing misfolded, damaged, or unneeded proteins .
The 26S proteasome is a large, multi-subunit complex composed of a 20S core particle and a 19S regulatory particle. PSMD5 is one of the non-ATPase subunits of the 19S regulatory particle. This subunit is involved in recognizing and binding ubiquitinated substrates, facilitating their translocation into the 20S core for degradation .
PSMD5, along with other subunits of the 26S proteasome, is essential for various cellular processes, including cell cycle regulation, signal transduction, and stress responses. The degradation of ubiquitinated proteins by the proteasome is a highly regulated process, ensuring that only proteins tagged for destruction are targeted, thus maintaining protein homeostasis .
Recombinant human PSMD5 is used in research to study the structure and function of the 26S proteasome. Advances in cryogenic electron microscopy (cryo-EM) have provided detailed insights into the dynamic organization and functional mechanisms of the proteasome, including the role of PSMD5 in substrate recognition and processing .