Ontology highlight
ABSTRACT:
SUBMITTER: Fu X
PROVIDER: S-EPMC6310792 | biostudies-literature | 2018 Dec
REPOSITORIES: biostudies-literature
Fu Xinyi X Sokolova Vladyslava V Webb Kristofor J KJ Old William W Park Soyeon S
Proceedings of the National Academy of Sciences of the United States of America 20181210 52
In the proteasome holoenzyme, the hexameric ATPases (Rpt1-Rpt6) enable degradation of ubiquitinated proteins by unfolding and translocating them into the proteolytic core particle. During early-stage proteasome assembly, individual Rpt proteins assemble into the hexameric "Rpt ring" through binding to their cognate chaperones: Nas2, Hsm3, Nas6, and Rpn14. Here, we show that Rpt ring assembly employs a specific ubiquitination-mediated control. An E3 ligase, Not4, selectively ubiquitinates Rpt5 du ...[more]