Evidence map›Paper›PMID 31795790›Full record

ArticleAutophagy2020

The GID ubiquitin ligase complex is a regulator of AMPK activity and organismal lifespan.

Huaize Liu, Jie Ding, Karl Köhnlein, Nadine Urban, Alessandro Ori, Pablo Villavicencio-Lorini, Peter Walentek, Lars-Oliver Klotz, Thomas Hollemann, Thorsten Pfirrmann

Open access · bronzeAbstract read
In one paragraph

Article in Autophagy, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
50citing papers in PubMed, 1 pooled it
5.6field-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

50 citing papers in PubMed, 1 synthesis or guideline pooled it, 72 citations in OpenAlex.

  1. Guideline
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  13. RANBP9 and RANBP10 cooperate in regulating non-small cell lung cancer proliferation.Journal of experimental & clinical cancer research : CR · 2025
    Article
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  16. Review
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  18. Article
  19. Article
  20. Muskelin acts as a substrate receptor of the highly regulatedbioRxiv : the preprint server for biology · 2024
    Article
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

10 authors at 4 institutions in 2 countries.

Huaize LiuInstitute of Physiological Chemistry, Martin-Luther University Halle-Wittenberg , Halle, Germany.
Jie DingInstitute of Physiological Chemistry, Martin-Luther University Halle-Wittenberg , Halle, Germany.
Karl KöhnleinInstitute of Nutritional Sciences, Friedrich Schiller University Jena , Jena, Germany.
Nadine UrbanInstitute of Nutritional Sciences, Friedrich Schiller University Jena , Jena, Germany.
Alessandro OriLeibniz Institute on Aging, Fritz Lipmann Institute (FLI) , Jena, Germany.ORCID 0000-0002-3046-0871
Pablo Villavicencio-LoriniInstitute of Human Genetics, Martin-Luther University Halle-Wittenberg , Halle, Germany.
Peter WalentekDivision of Genetics, Genomics and Development, Molecular and Cell Biology Department, University of California at Berkeley , Berkeley, USA.ORCID 0000-0002-2332-6068
Lars-Oliver KlotzInstitute of Nutritional Sciences, Friedrich Schiller University Jena , Jena, Germany.
Thomas HollemannInstitute of Physiological Chemistry, Martin-Luther University Halle-Wittenberg , Halle, Germany.
Thorsten PfirrmannInstitute of Physiological Chemistry, Martin-Luther University Halle-Wittenberg , Halle, Germany.
Martin Luther University Halle-Wittenberg · DEFriedrich Schiller University Jena · DELeibniz Institute on Aging - Fritz Lipmann Institute (FLI) · DEUniversity of Freiburg · DE

Funding

Molecular mechanisms of mucociliary function and airway clearanceK99HL127275 · NHLBI · UNIVERSITY OF CALIFORNIA BERKELEY · PI WALENTEK, PETER · 2016 to 2017
$268k
NHLBI NIH HHS K99 HL127275
6 · The paper itself

Abstract

The AMP-activated protein kinase (AMPK) regulates cellular energy homeostasis by sensing the metabolic status of the cell. AMPK is regulated by phosphorylation and dephosphorylation as a result of changing AMP/ATP levels and by removal of inhibitory ubiquitin residues by USP10. In this context, we identified the GID-complex, an evolutionarily conserved ubiquitin-ligase-complex (E3), as a negative regulator of AMPK activity. Our data show that the GID-complex targets AMPK for ubiquitination thereby altering its activity. Cells depleted of GID-subunits mimic a state of starvation as shown by increased AMPK activity and macroautophagic/autophagic flux as well as reduced MTOR activation. Consistently, ABBREVIATIONS: ACTB: actin, beta; ADP: adenosine diphosphate; AMP: adenosine monophosphate; AMPK: AMP-activated protein kinase; ARMC8: armadillo repeat containing 8; ATP: adenosine triphosphate; BafA1: bafilomycin A

Indexed as

Adaptation, PhysiologicalAdenosine TriphosphateAMP-Activated Protein KinasesAnimalsAutophagyCaenorhabditis elegansCaenorhabditis elegans ProteinsCiliaLongevityLysineMiceMultienzyme ComplexesNIH 3T3 CellsProteasome Endopeptidase ComplexProteolysisSignal TransductionAdenosine TriphosphateAMP-Activated Protein KinasesCaenorhabditis elegans ProteinsLysineMultienzyme ComplexesProteasome Endopeptidase ComplexTOR Serine-Threonine KinasesAMPKautophagyGIDlongevityprimary ciliumubiquitination

Identifiers

PMID31795790
PMCPMC8386601
OpenAlexW2994343164

What OpenQuestion holds

Textmetadata
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.