Journal
CELL
Volume 171, Issue 6, Pages 1326-+Publisher
CELL PRESS
DOI: 10.1016/j.cell.2017.10.016
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Funding
- Gordon and Betty Moore Foundation [GBMF775]
- Beckman Institute
- F32 grant [GM112308]
- Jane Coffin Childs Memorial Fund for Medical Research [61-1516]
- HHMI
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SCF (Skp1-Cullin-F-box) ubiquitin ligases comprise several dozen modular enzymes that have diverse roles in biological regulation. SCF enzymes share a common catalytic core containing Cul1, Rbx1, which is directed toward different substrates by a variable substrate receptor (SR) module comprising 1 of 69 F-box proteins bound to Skp1. Despite the broad cellular impact of SCF enzymes, important questions remain about the architecture and regulation of the SCF repertoire, including whether SRs compete for Cul1 and, if so, how this competition is managed. Here, we devise methods that preserve the in vivo assemblages of SCF complexes and apply quantitative mass spectrometry to perform a census of these complexes (the SCFome'') in various states. We show that Nedd8 conjugation and the SR exchange factor Cand1 have a profound effect on shaping the SCFome. Together, these factors enable rapid remodeling of SCF complexes to promote biased assembly of SR modules bound to substrate.
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