Journal
CURRENT OPINION IN STRUCTURAL BIOLOGY
Volume 21, Issue 2, Pages 257-264Publisher
CURRENT BIOLOGY LTD
DOI: 10.1016/j.sbi.2011.01.003
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Funding
- ALSAC
- St. Jude Cancer Center [P30CA021765]
- National Institutes of Health [R01 GM069530, R01 CA107134, F32 GM093497]
- Damon-Runyon Cancer Research Foundation [DRG 2021-9]
- Burroughs Wellcome Fund
- National Science Foundation
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Cullin-RING ligases (CRLs) compose the largest class of E3 ubiquitin ligases. CRLs are modular, multisubunit enzymes, comprising interchangeable substrate receptors dedicated to particular Cullin-RING catalytic cores. Recent structural studies have revealed numerous ways in which CRL E3 ligase activities are controlled, including multimodal E3 ligase activation by covalent attachment of the ubiquitin-like protein NEDD8, inhibition of CRL assembly/activity by CAND1, and several mechanisms of regulated substrate recruitment. These features highlight the potential for CRL activities to be tuned in responses to diverse cellular cues, and for modulating CRL functions through small-molecule agonists or antagonists. As the second installment of a two-review series, this article focuses on recent structural studies advancing our knowledge of how CRL activities are regulated.
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