Spatial mechanisms of quality control during chaperone-mediated assembly of the proteasome.

ABSTRACT: Cellular protein degradation requires a complex molecular machine, the proteasome. To mitigate the fundamental challenge of assembling the 66-subunit proteasome, cells utilize dedicated chaperones to order subunit addition. However, recent evidence suggests that proteasome assembly is not simply a series of subunit additions, but each step may be scrutinized so that only correct assembly events advance to proteasomes. Here, we find an unexpected mechanism of quality control (QC) during proteasome assembly-via the proteasomal nuclear localization signal (NLS). This mechanism specifically sequesters defective assembly intermediates to the nucleus, away from ongoing assembly in the cytoplasm, thereby antagonizing defective proteasome formation. This NLS, a bona fide proteasomal component, pro

SUBMITTER: Das E 

PROVIDER: S-EPMC11982566 | biostudies-literature | 2025 Apr

REPOSITORIES: biostudies-literature