Evidence map›Paper›PMID 37028429›Full record

ArticleCell2023

Systemwide disassembly and assembly of SCF ubiquitin ligase complexes.

Kheewoong Baek, Daniel C Scott, Lukas T Henneberg, Moeko T King, Matthias Mann, Brenda A Schulman

Erratum issuedOpen access · bronzeAbstract read
In one paragraph

Article in Cell, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
6.2field-weighted citation impact, top 3% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

27 citing papers in PubMed, 40 citations in OpenAlex.

  1. Article
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  9. Review
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  11. Article
  12. Review
  13. Reciprocal Regulation Between the SCFbioRxiv : the preprint server for biology · 2025
    Article
  14. Article
  15. SKP1-CUL1-F-box: Key molecular targets affecting disease progression.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2025
    Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors at 2 institutions in 2 countries.

Kheewoong BaekDepartment of Molecular Machines and Signaling, Max Planck Institute of Biochemistry, Martinsried 82152, Germany.
Daniel C ScottDepartment of Structural Biology, St. Jude Children's Research Hospital, Memphis, TN 38105, USA.
Lukas T HennebergDepartment of Molecular Machines and Signaling, Max Planck Institute of Biochemistry, Martinsried 82152, Germany.
Moeko T KingDepartment of Structural Biology, St. Jude Children's Research Hospital, Memphis, TN 38105, USA.
Matthias MannDepartment of Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, Martinsried, Germany.
Brenda A SchulmanDepartment of Molecular Machines and Signaling, Max Planck Institute of Biochemistry, Martinsried 82152, Germany; Department of Structural Biology, St. Jude Children's Research Hospital, Memphis, TN 38105, USA. Electronic address: schulman@biochem.mpg.de.
Max Planck Institute of Biochemistry · DESt. Jude Children's Research Hospital · US

Funding

Viral Vector Technology (VVTSR)P30CA021765 · NCI · ST. JUDE CHILDREN'S RESEARCH HOSPITAL · PI CHARLES ROBERTS · 1985 to 2026
$166.9M
Chemical Biology of the Control of Neddylation by DCN1R01CA247365 · NCI · UNIVERSITY OF KENTUCKY · PI GUY, RODNEY KIPLIN, SCHULMAN, BRENDA A · 2019 to 2023
$3.2M
NCI NIH HHS P30 CA021765NCI NIH HHS R01 CA247365
6 · The paper itself

Abstract

Cells respond to environmental cues by remodeling their inventories of multiprotein complexes. Cellular repertoires of SCF (SKP1-CUL1-F box protein) ubiquitin ligase complexes, which mediate much protein degradation, require CAND1 to distribute the limiting CUL1 subunit across the family of ∼70 different F box proteins. Yet, how a single factor coordinately assembles numerous distinct multiprotein complexes remains unknown. We obtained cryo-EM structures of CAND1-bound SCF complexes in multiple states and correlated mutational effects on structures, biochemistry, and cellular assays. The data suggest that CAND1 clasps idling catalytic domains of an inactive SCF, rolls around, and allosterically rocks and destabilizes the SCF. New SCF production proceeds in reverse, through SKP1-F box allosterically destabilizing CAND1. The CAND1-SCF conformational ensemble recycles CUL1 from inactive complexes, fueling mixing and matching of SCF parts for E3 activation in response to substrate availability. Our data reveal biogenesis of a predominant family of E3 ligases, and the molecular basis for systemwide multiprotein complex assembly.

Indexed as

Cullin ProteinsF-Box ProteinsSKP Cullin F-Box Protein LigasesTranscription FactorsHumansMolecular ConformationUbiquitin-Protein LigasesCAND1 protein, humanCullin 1Cullin ProteinsF-Box ProteinsSKP Cullin F-Box Protein LigasesTranscription FactorsUbiquitin-Protein LigasesCAND1CRLcryo-EMcullin-RING ligaseE3 ligaseNEDD8protein complex assemblyproteomicsSCFubiquitin

Identifiers

PMID37028429
PMCPMC10156175
OpenAlexW4362664589

What Socratic holds

Textmetadata
LicenceCC BY-NC
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the Socratic graph.