Ontology highlight
ABSTRACT:
SUBMITTER: Wu K
PROVIDER: S-EPMC4833235 | biostudies-literature | 2016 Apr
REPOSITORIES: biostudies-literature
Proceedings of the National Academy of Sciences of the United States of America 20160321 14
Cullin-RING E3 ubiquitin ligases (CRL) control a myriad of biological processes by directing numerous protein substrates for proteasomal degradation. Key to CRL activity is the recruitment of the E2 ubiquitin-conjugating enzyme Cdc34 through electrostatic interactions between E3's cullin conserved basic canyon and the acidic C terminus of the E2 enzyme. This report demonstrates that a small-molecule compound, suramin, can inhibit CRL activity by disrupting its ability to recruit Cdc34. Suramin, ...[more]