The DOI matches its Crossref record; 85 of the 85 references it cites were found in a registry or an index.
Structure of the Cand1-Cul1-Roc1 Complex Reveals Regulatory Mechanisms for the Assembly of the Multisubunit Cullin-Dependent Ubiquitin Ligases
Open accessAbstract
The SCF ubiquitin ligase complex regulates diverse cellular functions by ubiquitinating numerous protein substrates. Cand1, a 120 kDa HEAT repeat protein, forms a tight complex with the Cul1-Roc1 SCF catalytic core, inhibiting the assembly of the multisubunit E3 complex. The crystal structure of the Cand1-Cul1-Roc1 complex shows that Cand1 adopts a highly sinuous superhelical structure, clamping around the elongated SCF scaffold protein Cul1. At one end, a Cand1 beta hairpin protrusion partially occupies the adaptor binding site on Cul1, inhibiting its interactions with the Skp1 adaptor and the substrate-recruiting F box protein subunits. At the other end, two Cand1 HEAT repeats pack against a conserved Cul1 surface cleft and bury a Cul1 lysine residue, whose modification by the ubiquitin-like protein, Nedd8, is able to block Cand1-Cul1 association. Together with biochemical evidence, these structural results elucidate the mechanisms by which Cand1 and Nedd8 regulate the assembly-disassembly cycles of SCF and other cullin-dependent E3 complexes.
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Structural Studies of HHARI/UbcH7∼Ub Reveal Unique E2∼Ub Conformational Restriction by RBR RING1
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Metadata
- Authors
- Goldenberg, S. J., Cascio, T. C., Shumway, S. D., Garbutt, K. C., Liu, J., Xiong, Y., & Zheng, N.
- Affiliations
- University of Washington (US)
- University of North Carolina at Chapel Hill (US)
- Corresponding author
- Zheng, Ning
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2004-11
- Volume
- 119
- Issue
- 4
- Pages
- 517-528
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2094021381
- Cited by
- 280
- References
- 85
- Citations by year
- 2026: 2 · 2025: 7 · 2024: 5 · 2023: 14 · 2022: 7 · 2021: 8 · 2020: 14 · 2019: 11 · 2018: 5 · 2017: 14 · 2016: 16 · 2015: 8 · 2014: 11 · 2013: 27 · 2012: 19
- FWCI
- 4.62
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- www.elsevier.com/legal/tdmrep-license (tdm)
- www.elsevier.com/open-access/userlicense/1.0/ (vor, 3180 d)
- doi.org/10.15223/policy-017 (stm-asf)
- doi.org/10.15223/policy-037 (stm-asf)
- doi.org/10.15223/policy-012 (stm-asf)
- doi.org/10.15223/policy-029 (stm-asf)
- doi.org/10.15223/policy-004 (stm-asf)
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- Carolina Digital Repository (University of North Carolina at Chapel Hill) (submittedVersion)
- UNC Libraries
- Funders
- National Cancer Institute (R01CA107134, CA 107134)
- National Institute of General Medical Sciences (2 T32 GM07270-29, T32GM007270)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Degradation and Inhibitors
- Keywords
- SCF ubiquitin ligase, CAND1, CUL1, ROC1, HEAT repeats, NEDD8, F-box protein, crystal structure, protein complex formation, ubiquitination
- MeSH terms
- Carrier Proteins, Crystallization, Humans, Models, Molecular, Molecular Conformation, Protein Binding, Transcription Factors, Cell Cycle Proteins, Ubiquitin, Ubiquitin-Protein Ligase Complexes, Cullin Proteins, SKP Cullin F-Box Protein Ligases, Adaptor Proteins, Signal Transducing
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