Evidence map›Paper›PMID 25392302›Full record

ArticleMolecular biology of the cell2015

Kinetic control by limiting glutaredoxin amounts enables thiol oxidation in the reducing mitochondrial intermembrane space.

Kerstin Kojer, Valentina Peleh, Gaetano Calabrese, Johannes M Herrmann, Jan Riemer

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
4.0field-weighted citation impact, top 5% 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

39 citing papers in PubMed, 70 citations in OpenAlex.

  1. Redox signals and oxidative stress in the control of mitochondrial protein import.Protein science : a publication of the Protein Society · 2026
    Review
  2. In and out of the mitochondrial intermembrane space.Protein science : a publication of the Protein Society · 2026
    Review
  3. Review
  4. Review
  5. Oxidation ofAntioxidants (Basel, Switzerland) · 2023
    Article
  6. Real-Time Monitoring of Hydrogen Peroxide Levels in Yeast and Mammalian Cells.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  7. Review
  8. Review
  9. CHCHD4 (MIA40) and the mitochondrial disulfide relay system.Biochemical Society transactions · 2021
    Review
  10. Review
  11. Frontiers in physiology · 2021
    Article
  12. In Vivo Imaging with Genetically Encoded Redox Biosensors.International journal of molecular sciences · 2020
    Review
  13. Article
  14. Review
  15. Article
  16. The role of thiols in antioxidant systems.Free radical biology & medicine · 2019
    Review
  17. Mitochondrial proteins: from biogenesis to functional networks.Nature reviews. Molecular cell biology · 2019
    Review
  18. Disulfide reductase systems in liver.British journal of pharmacology · 2019
    Review
  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

5 authors at 1 institution in 1 country.

Kerstin KojerCellular Biochemistry, University of Kaiserslautern, 67663 Kaiserslautern, Germany.
Valentina PelehCell Biology, University of Kaiserslautern, 67663 Kaiserslautern, Germany.
Gaetano CalabreseCellular Biochemistry, University of Kaiserslautern, 67663 Kaiserslautern, Germany.
Johannes M HerrmannCell Biology, University of Kaiserslautern, 67663 Kaiserslautern, Germany.
Jan RiemerCellular Biochemistry, University of Kaiserslautern, 67663 Kaiserslautern, Germany jan.riemer@biologie.uni-kl.de.
University of Kaiserslautern · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The mitochondrial intermembrane space (IMS) harbors an oxidizing machinery that drives import and folding of small cysteine-containing proteins without targeting signals. The main component of this pathway is the oxidoreductase Mia40, which introduces disulfides into its substrates. We recently showed that the IMS glutathione pool is maintained as reducing as that of the cytosol. It thus remained unclear how equilibration of protein disulfides with the IMS glutathione pool is prevented in order to allow oxidation-driven protein import. Here we demonstrate the presence of glutaredoxins in the IMS and show that limiting amounts of these glutaredoxins provide a kinetic barrier to prevent the thermodynamically feasible reduction of Mia40 substrates by the IMS glutathione pool. Moreover, they allow Mia40 to exist in a predominantly oxidized state. Consequently, overexpression of glutaredoxin 2 in the IMS results in a more reduced Mia40 redox state and a delay in oxidative folding and mitochondrial import of different Mia40 substrates. Our findings thus indicate that carefully balanced glutaredoxin amounts in the IMS ensure efficient oxidative folding in the reducing environment of this compartment.

Indexed as

CytosolGlutaredoxinsGlutathioneGlutathione DisulfideImmunoblottingKineticsMetalloproteasesMitochondriaMitochondrial MembranesMitochondrial Membrane Transport ProteinsMitochondrial Precursor Protein Import Complex ProteinsMitochondrial ProteinsMolecular ChaperonesMutationOxidation-ReductionProtein TransportATP23 protein, S cerevisiaeCCS1 protein, S cerevisiaeGlutaredoxinsGlutathioneGlutathione DisulfideGrx2 protein, S cerevisiaeMetalloproteasesMIA40 protein, S cerevisiaeMitochondrial Membrane Transport ProteinsMitochondrial Precursor Protein Import Complex ProteinsMitochondrial ProteinsMolecular ChaperonesSaccharomyces cerevisiae ProteinsSulfhydryl Compounds

Identifiers

PMID25392302
PMCPMC4294668
OpenAlexW2148919897

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.