Proteasome 26S subunit non-ATPase 7 (PSMD7)

Proteasome 26S subunit non-ATPase 7 (PSMD7) is an essential non-ATPase regulatory subunit forming part of the lid of the 19S regulatory particle in the 26S proteasome complex, which is the primary apparatus for ATP/ubiquitin-dependent protein degradation in eukaryotic cells[1][3][4]. PSMD7 contains an MPN (Mpr1-Pad1 N-terminal) domain with a structure related to metalloproteases but lacking catalytic activity; instead, it serves a structural role by stabilizing the proteasome lid and facilitating its assembly[2]. The 26S proteasome, with PSMD7 as a core constituent, is vital for maintaining cellular protein homeostasis, regulating the cell cycle, apoptosis, and the degradation of damaged or misfolded proteins. It plays a pivotal part in antigen processing for immune surveillance, and its dysfunction has been implicated in cancer, neurodegenerative diseases like Alzheimer's disease, and potentially other disorders involving protein misfolding or turnover abnormalities[1][3][5]. While proteasome inhibitors are important in cancer therapy, these drugs typically target the proteolytic core and impact all regulatory subunits, including PSMD7, but there are no known drugs or biomarker assays specific for PSMD7 itself.

Other names

26S proteasome non-ATPase regulatory subunit 7PSMD7MOV34LS12P40MOV34Rpn826S proteasome regulatory subunit RPN826S proteasome regulatory subunit S12Mov34 protein homologProteasome subunit p40Mov34 homologMoloney leukemia virus-34 proviral integration

Proteasome inhibition (by drugs such as bortezomib and carfilzomib, which target the 20S core but also affect the whole 26S complex, leading to accumulation of ubiquitinated proteins and cell death, particularly in cancer cells)[5]