Evidence map›Paper›PMID 28426722›Full record

ArticlePloS one2017

Interactions between mitoNEET and NAF-1 in cells.

Ola Karmi, Sarah H Holt, Luhua Song, Sagi Tamir, Yuting Luo, Fang Bai, Ammar Adenwalla, Merav Darash-Yahana, Yang-Sung Sohn, Patricia A Jennings and 5 more

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
1.7field-weighted citation impact, top 17% 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

31 citing papers in PubMed, 53 citations in OpenAlex.

  1. Article
  2. The Labile Side of Iron in Health and Disease: A Narrative Review.Advances in experimental medicine and biology · 2025
    Review
  3. CISD3/MiNT is required for complex I function, mitochondrial integrity, and skeletal muscle maintenance.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  4. PINK1 and Parkin regulate IPNature communications · 2023
    Article
  5. ROS are evolutionary conserved cell-to-cell stress signals.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  6. Review
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Dysregulated CaCells · 2022
    Review
  14. Article
  15. Superoxide Radicals in the Execution of Cell Death.Antioxidants (Basel, Switzerland) · 2022
    Review
  16. Article
  17. Article
  18. Article
  19. 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

15 authors at 5 institutions in 2 countries.

Ola KarmiThe Alexander Silberman Institute of Life Science, Hebrew University of Jerusalem, Edmond J. Safra Campus at Givat Ram, Jerusalem, Israel.
Sarah H HoltDepartment of Biological Sciences and BioDiscovery Institute, University of North Texas, Denton, Texas, United States of America.
Luhua SongDepartment of Biological Sciences and BioDiscovery Institute, University of North Texas, Denton, Texas, United States of America.
Sagi TamirThe Alexander Silberman Institute of Life Science, Hebrew University of Jerusalem, Edmond J. Safra Campus at Givat Ram, Jerusalem, Israel.
Yuting LuoDepartment of Biological Sciences and BioDiscovery Institute, University of North Texas, Denton, Texas, United States of America.
Fang BaiCenter for Theoretical Biological Physics and Departments of Physics and Astronomy, Chemistry and Biosciences, Rice University, Houston, Texas, United States of America.
Ammar AdenwallaDepartments of Biological Sciences and Bioengineering, University of Texas at Dallas, Richardson, Texas, United States of America.
Merav Darash-YahanaThe Alexander Silberman Institute of Life Science, Hebrew University of Jerusalem, Edmond J. Safra Campus at Givat Ram, Jerusalem, Israel.
Yang-Sung SohnThe Alexander Silberman Institute of Life Science, Hebrew University of Jerusalem, Edmond J. Safra Campus at Givat Ram, Jerusalem, Israel.
Patricia A JenningsDepartment of Chemistry & Biochemistry, University of California at San Diego, La Jolla, California, United States of America.
Rajeev K AzadDepartment of Biological Sciences and BioDiscovery Institute, University of North Texas, Denton, Texas, United States of America.
Jose' N OnuchicCenter for Theoretical Biological Physics and Departments of Physics and Astronomy, Chemistry and Biosciences, Rice University, Houston, Texas, United States of America.
Faruck MorcosDepartments of Biological Sciences and Bioengineering, University of Texas at Dallas, Richardson, Texas, United States of America.
Rachel NechushtaiThe Alexander Silberman Institute of Life Science, Hebrew University of Jerusalem, Edmond J. Safra Campus at Givat Ram, Jerusalem, Israel.
Ron MittlerDepartment of Biological Sciences and BioDiscovery Institute, University of North Texas, Denton, Texas, United States of America.ORCID http://orcid.org/0000-0003-3192-7450
Hebrew University of Jerusalem · ILUniversity of North Texas · USCenter for Theoretical Biological Physics · USThe University of Texas at Dallas · USUniversity of California San Diego · US

Funding

Project# 4: INTERACTIONS OF ANCHORING PROTEINS WITH THEIR TARGETSP01DK054441 · NIDDK · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI TAYLOR, SUSAN S. · 1999 to 2017
$27.3M
NIDDK NIH HHS P01 DK054441
6 · The paper itself

Abstract

The NEET proteins mitoNEET (mNT) and nutrient-deprivation autophagy factor-1 (NAF-1) are required for cancer cell proliferation and resistance to oxidative stress. NAF-1 and mNT are also implicated in a number of other human pathologies including diabetes, neurodegeneration and cardiovascular disease, as well as in development, differentiation and aging. Previous studies suggested that mNT and NAF-1 could function in the same pathway in mammalian cells, preventing the over-accumulation of iron and reactive oxygen species (ROS) in mitochondria. Nevertheless, it is unknown whether these two proteins directly interact in cells, and how they mediate their function. Here we demonstrate, using yeast two-hybrid, in vivo bimolecular fluorescence complementation (BiFC), direct coupling analysis (DCA), RNA-sequencing, ROS and iron imaging, and single and double shRNA lines with suppressed mNT, NAF-1 and mNT/NAF-1 expression, that mNT and NAF-1 directly interact in mammalian cells and could function in the same cellular pathway. We further show using an in vitro cluster transfer assay that mNT can transfer its clusters to NAF-1. Our study highlights the possibility that mNT and NAF-1 function as part of an iron-sulfur (2Fe-2S) cluster relay to maintain the levels of iron and Fe-S clusters under control in the mitochondria of mammalian cells, thereby preventing the activation of apoptosis and/or autophagy and supporting cellular proliferation.

Indexed as

Cell LineHumansIronMembrane Potential, MitochondrialMembrane ProteinsMitochondriaMitochondrial ProteinsProtein BindingReactive Oxygen SpeciesRNA, MessengerSequence Analysis, RNATwo-Hybrid System TechniquesCISD1 protein, humanIronMembrane ProteinsMitochondrial ProteinsReactive Oxygen SpeciesRNA, Messenger

Identifiers

PMID28426722
PMCPMC5398536
OpenAlexW2605658575

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.