Evidence map›Paper›PMID 33905682›Full record

ArticleMolecular cell2021

GID E3 ligase supramolecular chelate assembly configures multipronged ubiquitin targeting of an oligomeric metabolic enzyme.

Dawafuti Sherpa, Jakub Chrustowicz, Shuai Qiao, Christine R Langlois, Laura A Hehl, Karthik Varma Gottemukkala, Fynn M Hansen, Ozge Karayel, Susanne von Gronau, J Rajan Prabu and 3 more

Open access · greenAbstract read
In one paragraph

Article in Molecular cell, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.

0numbers the graph read from it
0cells of the map it votes in
59citing papers in PubMed
5.2field-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

59 citing papers in PubMed, 91 citations in OpenAlex.

  1. Article
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  9. Review
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  12. Review
  13. Article
  14. Degrons: defining the rules of protein degradation.Nature reviews. Molecular cell biology · 2025
    Review
  15. The many faces of the GID/CTLH E3 ligase complex.Biochemical Society transactions · 2025
    Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. RANBP9 and RANBP10 cooperate in regulating non-small cell lung cancer proliferation.Journal of experimental & clinical cancer research : CR · 2025
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

13 authors at 1 institution in 1 country.

Dawafuti SherpaDepartment of Molecular Machines and Signaling, Max Planck Institute of Biochemistry, Martinsried 82152, Germany.
Jakub ChrustowiczDepartment of Molecular Machines and Signaling, Max Planck Institute of Biochemistry, Martinsried 82152, Germany.
Shuai QiaoDepartment of Molecular Machines and Signaling, Max Planck Institute of Biochemistry, Martinsried 82152, Germany.
Christine R LangloisDepartment of Molecular Machines and Signaling, Max Planck Institute of Biochemistry, Martinsried 82152, Germany.
Laura A HehlDepartment of Molecular Machines and Signaling, Max Planck Institute of Biochemistry, Martinsried 82152, Germany.
Karthik Varma GottemukkalaDepartment of Molecular Machines and Signaling, Max Planck Institute of Biochemistry, Martinsried 82152, Germany.
Fynn M HansenDepartment of Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, Martinsried 82152, Germany.
Ozge KarayelDepartment of Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, Martinsried 82152, Germany.
Susanne von GronauDepartment of Molecular Machines and Signaling, Max Planck Institute of Biochemistry, Martinsried 82152, Germany.
J Rajan PrabuDepartment of Molecular Machines and Signaling, Max Planck Institute of Biochemistry, Martinsried 82152, Germany.
Matthias MannDepartment of Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, Martinsried 82152, Germany.
Arno F AlpiDepartment of Molecular Machines and Signaling, Max Planck Institute of Biochemistry, Martinsried 82152, Germany.
Brenda A SchulmanDepartment of Molecular Machines and Signaling, Max Planck Institute of Biochemistry, Martinsried 82152, Germany. Electronic address: schulman@biochem.mpg.de.
Max Planck Institute of Biochemistry · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

How are E3 ubiquitin ligases configured to match substrate quaternary structures? Here, by studying the yeast GID complex (mutation of which causes deficiency in glucose-induced degradation of gluconeogenic enzymes), we discover supramolecular chelate assembly as an E3 ligase strategy for targeting an oligomeric substrate. Cryoelectron microscopy (cryo-EM) structures show that, to bind the tetrameric substrate fructose-1,6-bisphosphatase (Fbp1), two minimally functional GID E3s assemble into the 20-protein Chelator-GID

Indexed as

Adaptor Proteins, Signal TransducingAnimalsBinding SitesCell Adhesion MoleculesCryoelectron MicroscopyFructose-BisphosphataseGene ExpressionGluconeogenesisHumansIntracellular Signaling Peptides and ProteinsK562 CellsKineticsModels, MolecularMultienzyme ComplexesPromoter Regions, GeneticProtein BindingAdaptor Proteins, Signal TransducingCell Adhesion MoleculesFBP1 protein, S cerevisiaeFructose-BisphosphataseIntracellular Signaling Peptides and ProteinsMKLN1 protein, humanMultienzyme ComplexesRecombinant ProteinsSaccharomyces cerevisiae ProteinsUbiquitinUbiquitin-Conjugating Enzymesubiquitin-conjugating enzyme UBC8WDR26 protein, humancryo-EMCTLHE3GIDgluconeogenesismetabolic regulationRINGsupramolecular assemblyubiquitinubiquitin ligase

Identifiers

PMID33905682
PMCPMC8189437
OpenAlexW3151452178

What OpenQuestion holds

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LicenceCC BY-NC-ND
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 OpenQuestion graph.