Evidence map›Paper›PMID 29911972›Full record

ArticleeLife2018

The multi-subunit GID/CTLH E3 ubiquitin ligase promotes cell proliferation and targets the transcription factor Hbp1 for degradation.

Fabienne Lampert, Diana Stafa, Algera Goga, Martin Varis Soste, Samuel Gilberto, Natacha Olieric, Paola Picotti, Markus Stoffel, Matthias Peter

Open access · goldAbstract read
In one paragraph

Article in eLife, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 86 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
86citing papers in PubMed, 1 pooled it
5.8field-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

86 citing papers in PubMed, 1 synthesis or guideline pooled it, 137 citations in OpenAlex.

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  14. GSK3β Regulates a Novel β-Catenin Degradation Pathway via the GID Complex in Wnt Signaling.Genes to cells : devoted to molecular & cellular mechanisms · 2025
    Article
  15. The many faces of the GID/CTLH E3 ligase complex.Biochemical Society transactions · 2025
    Review
  16. Article
  17. RANBP9 and RANBP10 cooperate in regulating non-small cell lung cancer proliferation.Journal of experimental & clinical cancer research : CR · 2025
    Article
  18. Article
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26 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

9 authors at 4 institutions in 3 countries.

Fabienne Lampert *Institute of Biochemistry, ETH Zürich, Zürich, Switzerland.ORCID http://orcid.org/0000-0002-7560-4955
Diana Stafa *Institute of Biochemistry, ETH Zürich, Zürich, Switzerland.ORCID http://orcid.org/0000-0002-4177-0197
Algera GogaInstitute of Molecular Health Sciences, ETH Zürich, Zürich, Switzerland.
Martin Varis SosteInstitute of Biochemistry, ETH Zürich, Zürich, Switzerland.
Samuel GilbertoInstitute of Biochemistry, ETH Zürich, Zürich, Switzerland.
Natacha OliericLaboratory of Biomolecular Research, Division of Biology and Chemistry, Paul Scherrer Institute, Villigen, Switzerland.
Paola PicottiInstitute of Biochemistry, ETH Zürich, Zürich, Switzerland.
Markus StoffelInstitute of Molecular Health Sciences, ETH Zürich, Zürich, Switzerland.ORCID http://orcid.org/0000-0003-1304-5817
Matthias PeterInstitute of Biochemistry, ETH Zürich, Zürich, Switzerland.ORCID http://orcid.org/0000-0002-2160-6824
ETH Zurich · CHPaul Scherrer Institute · CHTulane University · USUniversity of Toronto · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In yeast, the glucose-induced degradation-deficient (GID) E3 ligase selectively degrades superfluous gluconeogenic enzymes. Here, we identified all subunits of the mammalian GID/CTLH complex and provide a comprehensive map of its hierarchical organization and step-wise assembly. Biochemical reconstitution demonstrates that the mammalian complex possesses inherent E3 ubiquitin ligase activity, using Ube2H as its cognate E2. Deletions of multiple GID subunits compromise cell proliferation, and this defect is accompanied by deregulation of critical cell cycle markers such as the retinoblastoma (Rb) tumor suppressor, phospho-Histone H3 and Cyclin A. We identify the negative regulator of pro-proliferative genes Hbp1 as a

Indexed as

Cell ProliferationAnimalsCell LineCells, CulturedG1 PhaseGene Expression RegulationHEK293 CellsHeLa CellsHigh Mobility Group ProteinsHumansMice, Inbred C57BLRepressor ProteinsTranscription FactorsUbiquitin-Conjugating EnzymesUbiquitin-Protein LigasesHBP1 protein, humanHigh Mobility Group ProteinsRepressor ProteinsTranscription FactorsUBE2E2 protein, humanUBE2H protein, humanUbiquitin-Conjugating EnzymesUbiquitin-Protein Ligasesbiochemistrycell biologycell proliferationchemical biologyE3 ubiquitin ligasehumanmetabolismmouseN-end ruleS. cerevisiaetranscription factors

Identifiers

PMID29911972
PMCPMC6037477
OpenAlexW2807773644

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.