Evidence map›Paper›PMID 38714719›Full record

ArticleNature communications2024

Structural basis for the intracellular regulation of ferritin degradation.

Fabian Hoelzgen, Thuy T P Nguyen, Elina Klukin, Mohamed Boumaiza, Ayush K Srivastava, Elizabeth Y Kim, Ran Zalk, Anat Shahar, Sagit Cohen-Schwartz, Esther G Meyron-Holtz and 3 more

Abstract read
In one paragraph

Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
–field-weighted citation impact
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

44 citing papers in PubMed.

  1. Review
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  9. Multivalent recognition of ferritin by full-length NCOA4 enables robust ferritinophagy.Protein science : a publication of the Protein Society · 2026
    Article
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  11. Review
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  16. The assembly rules guiding hetero-oligomeric bacterioferritin organization and their evolutionary signature.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  17. Review
  18. Review
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  20. Review
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

13 authors.

Fabian Hoelzgen *The Kreitman School of Advanced Graduate Studies, Marcus Family Campus, Ben-Gurion University of the Negev, Beer-Sheva, Israel.
Thuy T P Nguyen *Division of Radiation and Genome Stability, Department of Radiation Oncology, Dana-Farber Cancer Institute, Harvard Medical School, Boston, MA, USA.
Elina KlukinDepartment of Life Sciences, Marcus Family Campus, Ben-Gurion University of the Negev, Beer-Sheva, Israel.
Mohamed BoumaizaDepartment of Chemistry, State University of New York at Potsdam (SUNY Potsdam), Potsdam, NY, USA.
Ayush K SrivastavaDepartment of Chemistry, State University of New York at Potsdam (SUNY Potsdam), Potsdam, NY, USA.
Elizabeth Y KimDivision of Radiation and Genome Stability, Department of Radiation Oncology, Dana-Farber Cancer Institute, Harvard Medical School, Boston, MA, USA.
Ran ZalkIlse Katz Institute for Nanoscale Science & Technology, Marcus Family Campus, Ben-Gurion University of the Negev, Beer-Sheva, Israel.ORCID http://orcid.org/0000-0003-4251-6497
Anat ShaharIlse Katz Institute for Nanoscale Science & Technology, Marcus Family Campus, Ben-Gurion University of the Negev, Beer-Sheva, Israel.
Sagit Cohen-SchwartzThe National Institute for Biotechnology in the Negev - NIBN, Marcus Family Campus, Ben-Gurion University of the Negev, Beer-Sheva, Israel.
Esther G Meyron-HoltzFaculty of Biotechnology and Food Engineering, Technion, Haifa, Israel.
Fadi Bou-AbdallahDepartment of Chemistry, State University of New York at Potsdam (SUNY Potsdam), Potsdam, NY, USA.ORCID http://orcid.org/0000-0002-8557-1827
Joseph D ManciasDivision of Radiation and Genome Stability, Department of Radiation Oncology, Dana-Farber Cancer Institute, Harvard Medical School, Boston, MA, USA. Joseph_Mancias@dfci.harvard.edu.ORCID http://orcid.org/0000-0002-0692-3717
Gabriel A FrankDepartment of Life Sciences, Marcus Family Campus, Ben-Gurion University of the Negev, Beer-Sheva, Israel. frankg@bgu.ac.il.ORCID http://orcid.org/0000-0001-8379-5133

Funding

The role of NCOA4-mediated ferritinophagy in iron homeostasis and ferroptosisR01DK124384 · NIDDK · DANA-FARBER CANCER INST · PI MANCIAS, JOSEPH D · 2020 to 2024
$1.8M
NIDDK NIH HHS R01 DK124384
6 · The paper itself

Abstract

The interaction between nuclear receptor coactivator 4 (NCOA4) and the iron storage protein ferritin is a crucial component of cellular iron homeostasis. The binding of NCOA4 to the FTH1 subunits of ferritin initiates ferritinophagy-a ferritin-specific autophagic pathway leading to the release of the iron stored inside ferritin. The dysregulation of NCOA4 is associated with several diseases, including neurodegenerative disorders and cancer, highlighting the NCOA4-ferritin interface as a prime target for drug development. Here, we present the cryo-EM structure of the NCOA4-FTH1 interface, resolving 16 amino acids of NCOA4 that are crucial for the interaction. The characterization of mutants, designed to modulate the NCOA4-FTH1 interaction, is used to validate the significance of the different features of the binding site. Our results explain the role of the large solvent-exposed hydrophobic patch found on the surface of FTH1 and pave the way for the rational development of ferritinophagy modulators.

Indexed as

Cryoelectron MicroscopyFerritinsNuclear Receptor CoactivatorsAutophagyBinding SitesHEK293 CellsHumansIronModels, MolecularMutationOxidoreductasesProtein BindingProteolysisFerritinsFTH1 protein, humanIronNCOA4 protein, humanNuclear Receptor CoactivatorsOxidoreductases

Identifiers

PMID38714719
PMCPMC11076521

What OpenQuestion holds

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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.