Ontology highlight
ABSTRACT:
SUBMITTER: Gao H
PROVIDER: S-EPMC8861141 | biostudies-literature | 2022 Feb
REPOSITORIES: biostudies-literature
Cell discovery 20220222 1
The conserved ATPase p97 (Cdc48 in yeast) and adaptors mediate diverse cellular processes through unfolding polyubiquitinated proteins and extracting them from macromolecular assemblies and membranes for disaggregation and degradation. The tandem ATPase domains (D1 and D2) of the p97/Cdc48 hexamer form stacked rings. p97/Cdc48 can unfold substrates by threading them through the central pore. The pore loops critical for substrate unfolding are, however, not well-ordered in substrate-free p97/Cdc4 ...[more]