Journal
CURRENT OPINION IN STRUCTURAL BIOLOGY
Volume 67, Issue -, Pages 101-109Publisher
CURRENT BIOLOGY LTD
DOI: 10.1016/j.sbi.2020.10.007
Keywords
-
Categories
Funding
- NIH [R01CA247365, P30CA021765]
- St. Jude Children's Research Hospital
- ALSAC
- European Research Council (ERC) under the European Union's Horizon 2020 research and innovation programme [789016-NEDD8Activate]
- Deutsche Forschungsgemeinschaft (DFG, German Research Foundation) [SCHU 3196/1-1]
- Max Planck Society
Ask authors/readers for more resources
In summary, RING E3s are the largest family of ubiquitin and ubiquitin-like protein ligases, typically working with E2 enzymes to transfer UB or UBL to specific substrates. Multifunctional RING E3s like cullin-RING ligase family have been shown to interact with various E2s to target distinct proteins or transfer different UBLs. The recent structures of cullin-RING ligases and their partner E2 enzymes reveal multimodal mechanisms directing these enzyme active sites to modify specific targets.
RING E3s comprise the largest family of ubiquitin (UB) and ubiquitin-like protein (UBL) ligases. RING E3s typically promote UB or UBL transfer from the active site of an associated E2 enzyme to a distally-recruited substrate. Many RING E3s - including the cullin-RING ligase family - are multifunctional, interacting with various E2s (or other E3s) to target distinct proteins, transfer different UBLs, or to initially modify substrates with UB or subsequently elongate UB chains. Here we consider recent structures of cullin-RING ligases, and their partner E2 enzymes, representing ligation reactions. The studies collectively reveal multimodal mechanisms - interactions between ancillary E2 or E3 domains, post-translational modifications, or auxiliary binding partners - directing cullinRING E3-E2 enzyme active sites to modify their specific targets.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available