Evidence map›Paper›PMID 31784520›Full record

ArticleNature communications2019

Glycogen branching enzyme controls cellular iron homeostasis via Iron Regulatory Protein 1 and mitoNEET.

Nhan Huynh, Qiuxiang Ou, Pendleton Cox, Roland Lill, Kirst King-Jones

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
5.7field-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

29 citing papers in PubMed, 63 citations in OpenAlex.

  1. Article
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  7. In situ detection of ferric reductase activity in the intestinal lumen of an insect.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2024
    Article
  8. Redox report : communications in free radical research · 2024
    Article
  9. Article
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  13. An efficient injection protocol forBiology methods & protocols · 2024
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Molecular Mechanisms of Iron and Heme Metabolism.Annual review of nutrition · 2022
    Review
  20. 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

5 authors at 2 institutions in 2 countries.

Nhan HuynhDepartment of Biological Sciences, University of Alberta, G-504 Biological Sciences Bldg, Edmonton, Alberta, T6G 2E9, Canada.
Qiuxiang OuDepartment of Biological Sciences, University of Alberta, G-504 Biological Sciences Bldg, Edmonton, Alberta, T6G 2E9, Canada.
Pendleton CoxDepartment of Biological Sciences, University of Alberta, G-504 Biological Sciences Bldg, Edmonton, Alberta, T6G 2E9, Canada.
Roland LillInstitut für Zytobiologie und Zytopathologie, Philipps-Universität Marburg, Robert-Koch-Strasse 6, 35032, Marburg, Germany.ORCID http://orcid.org/0000-0002-8345-6518
Kirst King-JonesDepartment of Biological Sciences, University of Alberta, G-504 Biological Sciences Bldg, Edmonton, Alberta, T6G 2E9, Canada. kirst.king-jones@ualberta.ca.ORCID http://orcid.org/0000-0002-9089-8015
University of Alberta · CAPhilipps University of Marburg · DE

Funding

CIHR MOP 93761
6 · The paper itself

Abstract

Iron Regulatory Protein 1 (IRP1) is a bifunctional cytosolic iron sensor. When iron levels are normal, IRP1 harbours an iron-sulphur cluster (holo-IRP1), an enzyme with aconitase activity. When iron levels fall, IRP1 loses the cluster (apo-IRP1) and binds to iron-responsive elements (IREs) in messenger RNAs (mRNAs) encoding proteins involved in cellular iron uptake, distribution, and storage. Here we show that mutations in the Drosophila 1,4-Alpha-Glucan Branching Enzyme (AGBE) gene cause porphyria. AGBE was hitherto only linked to glycogen metabolism and a fatal human disorder known as glycogen storage disease type IV. AGBE binds specifically to holo-IRP1 and to mitoNEET, a protein capable of repairing IRP1 iron-sulphur clusters. This interaction ensures nuclear translocation of holo-IRP1 and downregulation of iron-dependent processes, demonstrating that holo-IRP1 functions not just as an aconitase, but throttles target gene expression in anticipation of declining iron requirements.

Indexed as

1,4-alpha-Glucan Branching EnzymeActive Transport, Cell NucleusAnimalsDown-RegulationDrosophilaDrosophila ProteinsEcdysteroidsEndocrine GlandsGene Expression RegulationGene Knock-In TechniquesGene Knockout TechniquesHemeIronIron Regulatory Protein 1Iron-Sulfur ProteinsLarva1,4-alpha-Glucan Branching EnzymeDrosophila ProteinsEcdysteroidsHemeIronIron Regulatory Protein 1Iron-Sulfur ProteinsMitochondrial ProteinsRNA, Messenger

Identifiers

PMID31784520
PMCPMC6884552
OpenAlexW2990450886

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.