Journal
EMBO REPORTS
Volume 14, Issue 12, Pages 1050-1061Publisher
WILEY
DOI: 10.1038/embor.2013.173
Keywords
cullin; ubiquitin; Nedd8; COP9 signalosome; E3 ligase; CAND1
Categories
Funding
- National Institutes of Health [RO1-AG11085, RO1-GM095567, RO1-NS083524]
- Schulman laboratory by ALSAC (American Lebanese Syrian Associated Charities) [R01GM069530, P30CA021765]
- Howard Hughes Medical Institute
- Damon Runyon Cancer Research [DRG 2061-10]
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Cullin-RING E3 ubiquitin ligases (CRLs) control a plethora of biological pathways through targeted ubiquitylation of signalling proteins. These modular assemblies use substrate receptor modules to recruit specific targets. Recent efforts have focused on understanding the mechanisms that control the activity state of CRLs through dynamic alterations in CRL architecture. Central to these processes are cycles of cullin neddylation and deneddylation, as well as exchange of substrate receptor modules to re-sculpt the CRL landscape, thereby responding to the cellular requirements to turn over distinct proteins in different contexts. This review is focused on how CRLs are dynamically controlled with an emphasis on how c-ullin neddylation cycles are integrated with receptor exchange. Keywords: cullin; ubiquitin; Nedd8; COP9 signalosome; E3 ligase; CAND1
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