Forgot Password

If you have forgotten your password you can enter your email here and get a temporary password sent to your email.

NEDD8 modification of CUL1 dissociates p120(CAND1), an inhibitor of CUL1-SKP1 binding and SCF ligases.

Cullin proteins assemble a large number of RING E3 ubiquitin ligases and regulate various physiological processes. Covalent modification of cullins by the ubiquitin-like protein NEDD8 activates cullin ligases through an as yet undefined mechanism. We show here that p120(CAND1) selectively binds to unneddylated CUL1 and is dissociated by CUL1 neddylation. CAND1 formed a ternary complex with CUL1 and ROC1. CAND1 dissociated SKP1 from CUL1 and inhibited SCF ligase activity in vitro. Suppression of CAND1 in vivo increased the level of the CUL1-SKP1 complex. We suggest that by restricting SKP1-CUL1 interaction, CAND1 regulated the assembly of productive SCF ubiquitin ligases, allowing a common CUL1-ROC core to be utilized by a large number of SKP1-F box-substrate subcomplexes.

Pubmed ID: 12504025


  • Liu J
  • Furukawa M
  • Matsumoto T
  • Xiong Y


Molecular cell

Publication Data

December 30, 2002

Associated Grants


Mesh Terms

  • Amino Acid Sequence
  • Bacterial Proteins
  • Carrier Proteins
  • Cell Cycle Proteins
  • Cullin Proteins
  • DNA-Binding Proteins
  • Enzyme Inhibitors
  • F-Box Proteins
  • Genes, myc
  • Humans
  • Kinetics
  • Ligases
  • Macromolecular Substances
  • Molecular Sequence Data
  • Mutagenesis, Site-Directed
  • Peptide Synthases
  • Recombinant Proteins
  • SKP Cullin F-Box Protein Ligases
  • Saccharomyces cerevisiae
  • Saccharomyces cerevisiae Proteins
  • Transcription Factors
  • Ubiquitins