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TitleStructural insights into the ubiquitylation strategy of the oligomeric CRL2 E3 ubiquitin ligase.
Journal, issue, pagesEMBO J, Vol. 43, Issue 6, Page 1089-1109, Year 2024
Publish dateFeb 15, 2024
AuthorsZonglin Dai / Ling Liang / Weize Wang / Peng Zuo / Shang Yu / Yaqi Liu / Xuyang Zhao / Yishuo Lu / Yan Jin / Fangting Zhang / Dian Ding / Weiwei Deng / Yuxin Yin /
PubMed AbstractCullin-RING E3 ubiquitin ligase (CRL) family members play critical roles in numerous biological processes and diseases including cancer and Alzheimer's disease. Oligomerization of CRLs has been ...Cullin-RING E3 ubiquitin ligase (CRL) family members play critical roles in numerous biological processes and diseases including cancer and Alzheimer's disease. Oligomerization of CRLs has been reported to be crucial for the regulation of their activities. However, the structural basis for its regulation and mechanism of its oligomerization are not fully known. Here, we present cryo-EM structures of oligomeric CRL2 in its unneddylated state, neddylated state in complex with BEX2 as well as neddylated state in complex with FNIP1/FLCN. These structures reveal that asymmetric dimerization of N8-CRL2 is critical for the ubiquitylation of BEX2 while FNIP1/FLCN is ubiquitylated by monomeric CRL2. Our data present an example of the asymmetric homo-dimerization of CRL. Taken together, this study sheds light on the ubiquitylation strategy of oligomeric CRL2 according to substrates with different scales.
External linksEMBO J / PubMed:38360992 / PubMed Central
MethodsEM (single particle)
Resolution3.63 - 4.2 Å
Structure data

35461

8ij1

EMDB-35461, PDB-8ij1:
Protomer 1 and 2 of the asymmetry trimer of the Cul2-Rbx1-EloBC-FEM1B ubiquitin ligase complex
Method: EM (single particle) / Resolution: 4.2 Å

36182

8je1

EMDB-36182, PDB-8je1:
An asymmetry dimer of the Cul2-Rbx1-EloBC-FEM1B ubiquitin ligase complexed with BEX2
Method: EM (single particle) / Resolution: 3.95 Å

36183

8je2

EMDB-36183, PDB-8je2:
Cryo-EM structure of neddylated Cul2-Rbx1-EloBC-FEM1B complexed with FNIP1-FLCN
Method: EM (single particle) / Resolution: 3.63 Å

Chemicals

ChemComp-ZN:
Unknown entry

Source
  • homo sapiens (human)
KeywordsLIGASE / Complex / E3 ubiquitin ligase / Cullin / Oligomer

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