Evidence map›Paper›PMID 25318675›Full record

ArticleMolecular biology of the cell2014

A discrete pathway for the transfer of intermembrane space proteins across the outer membrane of mitochondria.

Agnieszka Gornicka, Piotr Bragoszewski, Piotr Chroscicki, Lena-Sophie Wenz, Christian Schulz, Peter Rehling, Agnieszka Chacinska

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
2.0field-weighted citation impact, top 13% 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

36 citing papers in PubMed, 59 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. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. The Journey of Mitochondrial Protein Import and the Roadmap to Follow.International journal of molecular sciences · 2023
    Review
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Failure to Guard: Mitochondrial Protein Quality Control in Cancer.International journal of molecular sciences · 2021
    Review
  18. Review
  19. Article
  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

7 authors at 3 institutions in 2 countries.

Agnieszka GornickaInternational Institute of Molecular and Cell Biology, 02-109 Warsaw, Poland.
Piotr BragoszewskiInternational Institute of Molecular and Cell Biology, 02-109 Warsaw, Poland.
Piotr ChroscickiInternational Institute of Molecular and Cell Biology, 02-109 Warsaw, Poland.
Lena-Sophie WenzInstitut für Biochemie und Molekularbiologie, ZBMZ, Universität Freiburg, D-79104 Freiburg, Germany.
Christian SchulzDepartment of Cellular Biochemistry, University Medical Center Göttingen, D-37073 Göttingen, Germany.
Peter RehlingDepartment of Cellular Biochemistry, University Medical Center Göttingen, D-37073 Göttingen, Germany.
Agnieszka ChacinskaInternational Institute of Molecular and Cell Biology, 02-109 Warsaw, Poland achacinska@iimcb.gov.pl.
International Institute of Molecular and Cell Biology · PLUniversitätsmedizin Göttingen · DEUniversity of Freiburg · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mitochondrial proteins are synthesized on cytosolic ribosomes and imported into mitochondria with the help of protein translocases. For the majority of precursor proteins, the role of the translocase of the outer membrane (TOM) and mechanisms of their transport across the outer mitochondrial membrane are well recognized. However, little is known about the mode of membrane translocation for proteins that are targeted to the intermembrane space via the redox-driven mitochondrial intermembrane space import and assembly (MIA) pathway. On the basis of the results obtained from an in organello competition import assay, we hypothesized that MIA-dependent precursor proteins use an alternative pathway to cross the outer mitochondrial membrane. Here we demonstrate that this alternative pathway involves the protein channel formed by Tom40. We sought a translocation intermediate by expressing tagged versions of MIA-dependent proteins in vivo. We identified a transient interaction between our model substrates and Tom40. Of interest, outer membrane translocation did not directly involve other core components of the TOM complex, including Tom22. Thus MIA-dependent proteins take another route across the outer mitochondrial membrane that involves Tom40 in a form that is different from the canonical TOM complex.

Indexed as

Mitochondrial MembranesMitochondrial Membrane Transport ProteinsMitochondrial Precursor Protein Import Complex ProteinsMitochondrial ProteinsProtein TransportSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTetrahydrofolate DehydrogenaseMIA40 protein, S cerevisiaeMitochondrial Membrane Transport ProteinsMitochondrial Precursor Protein Import Complex ProteinsMitochondrial ProteinsSaccharomyces cerevisiae ProteinsTetrahydrofolate DehydrogenaseTom40 protein, S cerevisiae

Identifiers

PMID25318675
PMCPMC4263444
OpenAlexW2127107002

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.