Evidence map›Paper›PMID 17978092›Full record

ArticleMolecular biology of the cell2008

Precursor oxidation by Mia40 and Erv1 promotes vectorial transport of proteins into the mitochondrial intermembrane space.

Judith M Müller, Dusanka Milenkovic, Bernard Guiard, Nikolaus Pfanner, Agnieszka Chacinska

Erratum issuedAbstract read
In one paragraph

Article in Molecular biology of the cell, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
4.8field-weighted citation impact, top 4% 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

34 citing papers in PubMed, 82 citations in OpenAlex.

  1. Review
  2. Article
  3. Microbiology spectrum · 2021
    Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Retro-translocation of mitochondrial intermembrane space proteins.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  13. Role of membrane contact sites in protein import into mitochondria.Protein science : a publication of the Protein Society · 2015
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. The power of yeast to model diseases of the powerhouse of the cell.Frontiers in bioscience (Landmark edition) · 2013
    Review
  20. Article
4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

5 authors at 2 institutions in 2 countries.

Judith M MüllerInstitut für Biochemie und Molekularbiologie, Zentrum für Biochemie und Molekulare Zellforschung, Universität Freiburg, D-79104 Freiburg, Germany.
Dusanka Milenkovic
Bernard Guiard
Nikolaus Pfanner
Agnieszka Chacinska
University of Freiburg · DECentre de Génétique Moléculaire · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The mitochondrial intermembrane space contains chaperone complexes that guide hydrophobic precursor proteins through this aqueous compartment. The chaperones consist of hetero-oligomeric complexes of small Tim proteins with conserved cysteine residues. The precursors of small Tim proteins are synthesized in the cytosol. Import of the precursors requires the essential intermembrane space proteins Mia40 and Erv1 that were proposed to form a relay for disulfide formation in the precursor proteins. However, experimental evidence for a role of Mia40 and Erv1 in the oxidation of intermembrane space precursors has been lacking. We have established a system to directly monitor the oxidation of precursors during import into mitochondria and dissected distinct steps of the import process. Reduced precursors bind to Mia40 during translocation into mitochondria. Both Mia40 and Erv1 are required for formation of oxidized monomers of the precursors that subsequently assemble into oligomeric complexes. Whereas the reduced precursors can diffuse back into the cytosol, the oxidized precursors are retained in the intermembrane space. Thus, oxidation driven by Mia40 and Erv1 determines vectorial transport of the precursors into the mitochondrial intermembrane space.

Indexed as

CysteineDisulfidesMembrane Transport ProteinsMitochondriaMitochondrial MembranesMitochondrial Membrane Transport ProteinsMitochondrial Precursor Protein Import Complex ProteinsMitochondrial ProteinsMutationOxidation-ReductionOxidoreductases Acting on Sulfur Group DonorsProtein PrecursorsProtein TransportSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsCysteineDisulfidesERV1 protein, S cerevisiaeMembrane Transport ProteinsMIA40 protein, S cerevisiaeMitochondrial Membrane Transport ProteinsMitochondrial Precursor Protein Import Complex ProteinsMitochondrial ProteinsOxidoreductases Acting on Sulfur Group DonorsProtein PrecursorsSaccharomyces cerevisiae ProteinsTim8 protein, S cerevisiae

Identifiers

PMID17978092
PMCPMC2174169
OpenAlexW2066009906

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.