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    J Biol Chem. 2011 Sep 16;286(37):32355-65. Epub 2011 Jul 21.

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

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

    Source

    Department of Internal Medicine, University of Texas Southwestern Medical Center, Dallas, Texas 75390, USA.

    Abstract

    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.

    PMID:
    21778237
    [PubMed - indexed for MEDLINE]
    PMCID:
    PMC3173175
    [Available on 2012/9/16]

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