Structure of the Cand1-Cul1-Roc1 Complex Reveals Regulatory Mechanisms for the Assembly of the Multisubunit Cullin-Dependent Ubiquitin Ligases

@article{Goldenberg2004StructureOT,
  title={Structure of the Cand1-Cul1-Roc1 Complex Reveals Regulatory Mechanisms for the Assembly of the Multisubunit Cullin-Dependent Ubiquitin Ligases},
  author={Seth J. Goldenberg and Thomas C. Cascio and Stuart D. Shumway and Kenneth C. Garbutt and Jidong Liu and Yue Xiong and Ning Zheng},
  journal={Cell},
  year={2004},
  volume={119},
  pages={517-528}
}

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The structure of the Cul1–Rbx1–Skp1–F boxSkp2 SCF complex suggests that Cul1 may contribute to catalysis through the positioning of the substrate and the ubiquitin-conjugating enzyme, and this model is supported by Cul1 mutations designed to eliminate the rigidity of the scaffold.
CAND1 binds to unneddylated CUL1 and regulates the formation of SCF ubiquitin E3 ligase complex.
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TLDR
It is shown that Cul3, but not other cullins, binds directly to multiple BTB domains through a conserved amino-terminal domain, suggesting that in vivo there exists a potentially large number of BCR3 (BTB–Cul3–Roc1) E3 ubiquitin ligases.
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TLDR
It is suggested that RING-E2, rather than cullin-RING, constitutes the catalytic core of the ubiquitin ligase and that one major function of the cullin subunit is to assemble the RING -E2 catalyticcore and substrates together.
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TLDR
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