• Register
X
Forgot Password

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

X

Leaving Community

Are you sure you want to leave this community? Leaving the community will revoke any permissions you have been granted in this community.

No
Yes

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

Authors

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

Journal

Molecular cell

Publication Data

December 30, 2002

Associated Grants

None

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