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TitleA conserved N-terminal motif of CUL3 contributes to assembly and E3 ligase activity of CRL3.
Journal, issue, pagesNat Commun, Vol. 15, Issue 1, Page 3789, Year 2024
Publish dateMay 6, 2024
AuthorsWeize Wang / Ling Liang / Zonglin Dai / Peng Zuo / Shang Yu / Yishuo Lu / Dian Ding / Hongyi Chen / Hui Shan / Yan Jin / Youdong Mao / Yuxin Yin /
PubMed AbstractThe CUL3-RING E3 ubiquitin ligases (CRL3s) play an essential role in response to extracellular nutrition and stress stimuli. The ubiquitin ligase function of CRL3s is activated through dimerization. ...The CUL3-RING E3 ubiquitin ligases (CRL3s) play an essential role in response to extracellular nutrition and stress stimuli. The ubiquitin ligase function of CRL3s is activated through dimerization. However, how and why such a dimeric assembly is required for its ligase activity remains elusive. Here, we report the cryo-EM structure of the dimeric CRL3 complex and reveal a conserved N-terminal motif in CUL3 that contributes to the dimerization assembly and the E3 ligase activity of CRL3. We show that deletion of the CUL3 N-terminal motif impairs dimeric assembly and the E3 ligase activity of both CRL3 and several other CRL3s. In addition, we found that the dynamics of dimeric assembly of CRL3 generates a variable ubiquitination zone, potentially facilitating substrate recognition and ubiquitination. These findings demonstrate that a CUL3 N-terminal motif participates in the assembly process and provide insights into the assembly and activation of CRL3s.
External linksNat Commun / PubMed:38710693 / PubMed Central
MethodsEM (single particle)
Resolution3.4 - 4.2 Å
Structure data

36961

8k8t

EMDB-36961, PDB-8k8t:
Structure of CUL3-RBX1-KLHL22 complex
Method: EM (single particle) / Resolution: 3.8 Å

36987

8k9i

EMDB-36987, PDB-8k9i:
Structure of CUL3-RBX1-KLHL22 complex without CUL3 NA motif
Method: EM (single particle) / Resolution: 4.2 Å

EMDB-39719: Focused map of CUL3-RBX1-KLHL22 dimerization region
Method: EM (single particle) / Resolution: 3.4 Å

EMDB-39720: Consensus map of CUL3-RBX1-KLHL22 complex
Method: EM (single particle) / Resolution: 3.8 Å

EMDB-39725: Cryo-EM structure of CUL3-RBX1-KLHL22 complex --C1 Symmetry
Method: EM (single particle) / Resolution: 3.7 Å

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

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