Evidence map›Paper›PMID 28637866›Full record

ArticleThe Journal of biological chemistry2017

Endoplasmic reticulum-mitochondria junction is required for iron homeostasis.

Yong Xue, Stefan Schmollinger, Narsis Attar, Oscar A Campos, Maria Vogelauer, Michael F Carey, Sabeeha S Merchant, Siavash K Kurdistani

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing 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

34 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Functional role ofVirulence · 2025
    Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Review
  10. Metal Ion Signaling in Biomedicine.Chemical reviews · 2025
    Review
  11. Towards a Unitary Hypothesis of Alzheimer's Disease Pathogenesis.Journal of Alzheimer's disease : JAD · 2024
    Article
  12. Review
  13. Review
  14. Article
  15. Heme sensing and trafficking in fungi.Fungal biology reviews · 2023
    Article
  16. Review
  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

8 authors.

Yong XueFrom the Department of Biological Chemistry.
Stefan SchmollingerInstitute for Genomics and Proteomics, Department of Chemistry and Biochemistry, UCLA, Los Angeles, California 90095 and.
Narsis AttarFrom the Department of Biological Chemistry.
Oscar A CamposFrom the Department of Biological Chemistry.
Maria VogelauerFrom the Department of Biological Chemistry.
Michael F CareyFrom the Department of Biological Chemistry.
Sabeeha S MerchantInstitute for Genomics and Proteomics, Department of Chemistry and Biochemistry, UCLA, Los Angeles, California 90095 and.
Siavash K KurdistaniFrom the Department of Biological Chemistry, skurdistani@mednet.ucla.edu.

Funding

Interplay Between Chromatin and Co-Activator ComplexesR01GM074701 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI CAREY, MICHAEL F · 2005 to 2025
$6.7M
Dynamics of Histone Acetylation in Cancer Cell PhysiologyR01CA178415 · NCI · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI KURDISTANI, SIAVASH · 2013 to 2017
$1.6M
NCI NIH HHS R01 CA178415NIGMS NIH HHS R01 GM074701
6 · The paper itself

Abstract

The endoplasmic reticulum (ER)-mitochondria encounter structure (ERMES) is a protein complex that physically tethers the two organelles to each other and creates the physical basis for communication between them. ERMES functions in lipid exchange between the ER and mitochondria, protein import into mitochondria, and maintenance of mitochondrial morphology and genome. Here, we report that ERMES is also required for iron homeostasis. Loss of ERMES components activates an Aft1-dependent iron deficiency response even in iron-replete conditions, leading to accumulation of excess iron inside the cell. This function is independent of known ERMES roles in calcium regulation, phospholipid biosynthesis, or effects on mitochondrial morphology. A mutation in the vacuolar protein sorting 13 (

Indexed as

Models, BiologicalAllelesAmino Acid SubstitutionEndoplasmic ReticulumEnergy MetabolismGene DeletionGene Expression Regulation, FungalHomeostasisIronMembrane ProteinsMitochondriaPoint MutationProtein TransportRNA, FungalRNA, MessengerSaccharomyces cerevisiaeIronMembrane ProteinsRNA, FungalRNA, MessengerSaccharomyces cerevisiae ProteinsSAM37 protein, S cerevisiaeVPS13 protein, S cerevisiaeendoplasmic reticulum (ER)iron metabolismmitochondriaprotein importrespiration

Identifiers

PMID28637866
PMCPMC5555183

What OpenQuestion holds

Textmetadata
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.