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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TLDR
The neddylation level of CUL-2 and Cul-4 in cand-1 mutant and found that the level of neddolation increased substantially for both cullins, indicating that CAND-1 negatively regulates neddYLation in vivo.
Cand1 Promotes Assembly of New SCF Complexes through Dynamic Exchange of F Box Proteins
Substrate-mediated Regulation of Cullin Neddylation*
TLDR
The critical role of substrate binding to promote Cul2 neddylation is demonstrated in a manner that does not require substrate ubiquitination but may involve a conformational change, suggesting a mechanism through which availability of substrate recognition subunits and substrates can regulate the ubiquitin ligase activity.
Regulation of Cullin RING E3 Ubiquitin Ligases by CAND1 In Vivo
TLDR
This study suggests that CAND1 does not function by sequestering cullins in vivo to prevent substrate receptor autoubiquitination and is likely to regulate cullin RING ligase activity via alternative mechanisms.
Structural Insights into NEDD8 Activation of Cullin-RING Ligases: Conformational Control of Conjugation
Association of SAP130/SF3b-3 with Cullin-RING ubiquitin ligase complexes and its regulation by the COP9 signalosome
TLDR
SAP130 is a cullin binding protein that is likely involved in the Nedd8 pathway and hypothesis that SAP130 may link CRL mediated ubiquitination to gene expression is hypothesis.
Crystal Structure of the Cul2-Rbx1-EloBC-VHL Ubiquitin Ligase Complex
Drosophila Cand1 regulates Cullin3-dependent E3 ligases by affecting the neddylation of Cullin3 and by controlling the stability of Cullin3 and adaptor protein.
The cullin protein family
TLDR
Genetic studies in several model organisms have helped to unravel a multitude of physiological functions associated with cullin proteins and their respective CRLs, which have an impact on a range of biological processes, including cell growth, development, signal transduction, transcriptional control, genomic integrity and tumor suppression.
Genetic analysis of CAND1–CUL1 interactions in Arabidopsis supports a role for CAND1-mediated cycling of the SCFTIR1 complex
TLDR
The fact that both decreased and increased CAND1–CUL1 interactions result in reduced SCFTIR1 activity in vivo strongly supports the hypothesis that CAND 1-mediated cycling is required for optimal SCF function.
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References

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TLDR
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NEDD8 modification of CUL1 dissociates p120(CAND1), an inhibitor of CUL1-SKP1 binding and SCF ligases.
CAND1 binds to unneddylated CUL1 and regulates the formation of SCF ubiquitin E3 ligase complex.
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TLDR
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TLDR
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TLDR
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TLDR
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TLDR
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TLDR
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