Cited by 280Ubiquitin and proteasome pathwaysEnzyme Structure and FunctionProtein Degradation and Inhibitors

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Structure of the Cand1-Cul1-Roc1 Complex Reveals Regulatory Mechanisms for the Assembly of the Multisubunit Cullin-Dependent Ubiquitin Ligases

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Goldenberg, Seth J., Cascio, Thomas C., Shumway, Stuart D., Garbutt, Kenneth C., Liu, Jidong, Xiong, Yue, Zheng, Ning·2004·Cell

DOI 10.1016/j.cell.2004.10.019

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Abstract

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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Research works printed but not linked: 1

CCP4, 1994, Collaborative Computational Project, Number 4) The CCP4 suite, Acta Crystallogr. D Biol. Crystallogr, 50, 760

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RING Domain E3 Ubiquitin Ligases
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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
ORCID: Liu, Jidong
Xiong, Yue
Zheng, Ning
Venue: Cell
Publisher: Elsevier BV
Published: 2004-11
Volume: 119
Issue: 4
Pages: 517-528
ISSN: 0092-8674 (ISSN-L)
DOI: 10.1016/j.cell.2004.10.019
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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Structure of the Cand1-Cul1-Roc1 Complex Reveals Regulatory Mechanisms for the Assembly of the Multisubunit Cullin-Dependent Ubiquitin Ligases

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