Proteasome assembly chaperone 4 (PAC4)

Proteasome assembly chaperone 4 (PAC4) is one of five dedicated chaperones required for the orderly biogenesis of the 20S core particle of the eukaryotic proteasome. PAC4 binds and temporarily associates with other chaperones (notably PAC3, forming a heterodimer), facilitating the arrangement of the seven distinct α subunits into a correct α-ring configuration during early proteasome assembly. After this, PAC4 dissociates as β subunits are incorporated. Understanding PAC4’s structure and function is ongoing, but it is emerging as a potential drug target for anticancer therapies aiming to inhibit proteasome assembly specifically in cancer cells, which demand increased protein degradation capacity.

Other names

PAC4Pba4

Inhibition of assembly chaperone function, thereby blocking the formation of the proteasome core particle and reducing proteasome activity in cells (especially cancer)