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COMMD1 (copper metabolism MURR1 domain-containing protein 1) regulates Cullin RING ligases by preventing CAND1 (Cullin-associated Nedd8-dissociated protein 1) binding.

Cullin RING ligases (CRLs), the most prolific class of ubiquitin ligase enzymes, are multimeric complexes that regulate a wide range of cellular processes. CRL activity is regulated by CAND1 (Cullin-associated Nedd8-dissociated protein 1), an inhibitor that promotes the dissociation of substrate receptor components from the CRL. We demonstrate here that COMMD1 (copper metabolism MURR1 domain-containing 1), a factor previously found to promote ubiquitination of various substrates, regulates CRL activation by antagonizing CAND1 binding. We show that COMMD1 interacts with multiple Cullins, that the COMMD1-Cul2 complex cannot bind CAND1, and that, conversely, COMMD1 can actively displace CAND1 from CRLs. These findings highlight a novel mechanism of CRL activation and suggest that CRL regulation may underlie the pleiotropic activities of COMMD1.

Pubmed ID: 21778237


  • Mao X
  • Gluck N
  • Chen B
  • Starokadomskyy P
  • Li H
  • Maine GN
  • Burstein E


The Journal of biological chemistry

Publication Data

September 16, 2011

Associated Grants

  • Agency: NIDDK NIH HHS, Id: R01 DK073639

Mesh Terms

  • Adaptor Proteins, Signal Transducing
  • Cullin Proteins
  • HEK293 Cells
  • HeLa Cells
  • Humans
  • Multiprotein Complexes
  • Protein Binding
  • Transcription Factors