Copper metabolism MURR1 domain containing 1 (COMMD1) regulates Cullin-RING ligases by preventing Cullin-associated NEDD8-dissociated (CAND1) binding.

Cullin-RING ligases (CRLs), the most prolific class of ubiquitin ligase enzymes, are multimeric complexes that regulate multiple cellular processes. CRL activity is regulated by Cullin-associated Nedd8-dissociated protein 1 (CAND1), an inhibitor that promotes the dissociation of substrate receptor components from the CRL. We demonstrate here that Copper metabolism MURR1 domain ...
containing 1 (COMMD1), 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.
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Date: Jul. 21, 2011
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