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TitleThe CRL4 cullin-RING ubiquitin ligase is activated following a switch in oligomerization state.
Journal, issue, pagesEMBO J, Vol. 40, Issue 22, Page e108008, Year 2021
Publish dateNov 15, 2021
AuthorsWeaam I Mohamed / Andreas D Schenk / Georg Kempf / Simone Cavadini / Anja Basters / Alessandro Potenza / Wassim Abdul Rahman / Julius Rabl / Kurt Reichermeier / Nicolas H Thomä /
PubMed AbstractThe cullin-4-based RING-type (CRL4) family of E3 ubiquitin ligases functions together with dedicated substrate receptors. Out of the ˜29 CRL4 substrate receptors reported, the DDB1- and CUL4- ...The cullin-4-based RING-type (CRL4) family of E3 ubiquitin ligases functions together with dedicated substrate receptors. Out of the ˜29 CRL4 substrate receptors reported, the DDB1- and CUL4-associated factor 1 (DCAF1) is essential for cellular survival and growth, and its deregulation has been implicated in tumorigenesis. We carried out biochemical and structural studies to examine the structure and mechanism of the CRL4 ligase. In the 8.4 Å cryo-EM map of CRL4 , four CUL4-RBX1-DDB1-DCAF1 protomers are organized into two dimeric sub-assemblies. In this arrangement, the WD40 domain of DCAF1 mediates binding with the cullin C-terminal domain (CTD) and the RBX1 subunit of a neighboring CRL4 protomer. This renders RBX1, the catalytic subunit of the ligase, inaccessible to the E2 ubiquitin-conjugating enzymes. Upon CRL4 activation by neddylation, the interaction between the cullin CTD and the neighboring DCAF1 protomer is broken, and the complex assumes an active dimeric conformation. Accordingly, a tetramerization-deficient CRL4 mutant has higher ubiquitin ligase activity compared to the wild-type. This study identifies a novel mechanism by which unneddylated and substrate-free CUL4 ligases can be maintained in an inactive state.
External linksEMBO J / PubMed:34595758 / PubMed Central
MethodsEM (single particle)
Resolution8.4 - 23.0 Å
Structure data

12964

7okq

EMDB-12964, PDB-7okq:
Cryo-EM Structure of the DDB1-DCAF1-CUL4A-RBX1 Complex
Method: EM (single particle) / Resolution: 8.4 Å

EMDB-12965:
Cryo-EM Structure of the DDB1-DCAF1-CUL4A-RBX1-CSN Complex
Method: EM (single particle) / Resolution: 23.0 Å

Source
  • homo sapiens (human)
KeywordsLIGASE / ubiquitin / E3 / protein degradation

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