PSMG4 functions as a chaperone protein that promotes the assembly of the 20S proteasome by partnering with another chaperone protein, PSMG3 . The assembly of the 20S proteasome is a multistep, ordered process that requires the assistance of chaperone proteins to ensure proper maturation and functionality . Specifically, PSMG4 and PSMG3 form a heterodimeric complex that interacts with precursor forms of proteasome subunits, facilitating their proper folding and assembly into the mature 20S proteasome .
The 20S proteasome is the catalytic core of the 26S proteasome complex, which is responsible for degrading misfolded, damaged, or regulatory proteins tagged with ubiquitin . This degradation process is vital for maintaining cellular homeostasis and regulating various cellular functions. Defects in proteasome assembly or function can lead to the accumulation of damaged proteins, contributing to the development of various diseases, including neurodegenerative disorders and cancers .
Mutations or dysregulation of the PSMG4 gene have been associated with several genetic disorders, including Robinow Syndrome, Autosomal Dominant 2, and Intellectual Developmental Disorder, Autosomal Recessive 74 . Understanding the role of PSMG4 in proteasome assembly and function can provide insights into the molecular mechanisms underlying these disorders and potentially lead to the development of targeted therapies.
Recombinant human PSMG4 is used in various research applications to study its role in proteasome assembly and function. By expressing and purifying recombinant PSMG4, researchers can investigate its interactions with other proteasome subunits and chaperone proteins, as well as its impact on proteasome activity and cellular processes .