Cand1 Promotes Assembly of New SCF Complexes through Dynamic Exchange of F Box Proteins
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The modular SCF (Skp1, cullin, and F box) ubiquitin ligases feature a large family of F box protein substrate receptors that enable recognition of diverse targets. However, how the repertoire of SCF complexes is sustained remains unclear. Real-time measurements of formation and disassembly indicate that SCF(Fbxw7) is extraordinarily stable, but, in the Nedd8-deconjugated state, the cullin-binding protein Cand1 augments its dissociation by one-million-fold. Binding and ubiquitylation assays show that Cand1 is a protein exchange factor that accelerates the rate at which Cul1-Rbx1 equilibrates with multiple F box protein-Skp1 modules. Depletion of Cand1 from cells impedes recruitment of new F box proteins to pre-existing Cul1 and profoundly alters the cellular landscape of SCF complexes. We suggest that catalyzed protein exchange may be a general feature of dynamic macromolecular machines and propose a hypothesis for how substrates, Nedd8, and Cand1 collaborate to regulate the cellular repertoire of SCF complexes.
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NEDD8 stabilizes cellular CRLs by blocking the exchange factor CAND1 from ejecting substrate receptors from unneddylated CUL-RBX complexes.
“NEDD8 also stabilizes cellular CRLs by blocking the exchange factor CAND1 from ejecting substrate receptors from unneddylated CUL-RBX complexes13.”
From NEDD8 nucleates a multivalent cullin–RING–UBE2D ubiquitin ligation assembly (2020) · cites this paper as [13]
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- Authors
- Pierce, N. W., Lee, J. E., Liu, X., Sweredoski, M. J., Graham, R. L. J., Larimore, E. A., Rome, M., Zheng, N., Clurman, B. E., Hess, S., Shan, S.-O., & Deshaies, R. J.
- Affiliations
- California Institute of Technology (US)
- University of Washington (US)
- Howard Hughes Medical Institute (US)
- Fred Hutch Cancer Center (US)
- Corresponding author
- Deshaies, Raymond J.
- ORCID
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2013-03
- Volume
- 153
- Issue
- 1
- Pages
- 206-215
- ISSN
- 0092-8674 (ISSN-L)
- PMC
- PMC3656483
- OpenAlex
- W2149650548
- Cited by
- 262
- References
- 48
- Citations by year
- 2026: 10 · 2025: 13 · 2024: 13 · 2023: 22 · 2022: 28 · 2021: 18 · 2020: 23 · 2019: 16 · 2018: 19 · 2017: 21 · 2016: 25 · 2015: 21 · 2014: 20 · 2013: 13
- FWCI
- 11.79
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- CaltechAUTHORS (California Institute of Technology) (submittedVersion)
- Research Explorer (The University of Manchester) (submittedVersion)
- Research Portal (Queen's University Belfast) (submittedVersion)
- Funders
- Howard Hughes Medical Institute
- Gordon and Betty Moore Foundation
- California Institute of Technology
- National Institutes of Health
- U.S. Public Health Service (10565784)
- National Cancer Institute (F32CA138126, R01CA084069, CA138126, T32CA080416)
- National Institute of General Medical Sciences (R01GM065997, GM065997)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Degradation and Inhibitors
- Keywords
- CAND1, SCF ubiquitin ligase, F-box protein, FBXW7, CUL1, RBX1, NEDD8, protein exchange, Skp1, protein disassembly, substrate recognition
- MeSH terms
- Animals, Cell Line, Escherichia coli, Humans, Mass Spectrometry, Transcription Factors, F-Box Proteins, Cullin Proteins, SKP Cullin F-Box Protein Ligases
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