Evidence map›Paper›PMID 25002531›Full record

ArticleMolecular and cellular biology2014

Presequence recognition by the tom40 channel contributes to precursor translocation into the mitochondrial matrix.

Jonathan Melin, Christian Schulz, Lidia Wrobel, Olaf Bernhard, Agnieszka Chacinska, Olaf Jahn, Bernhard Schmidt, Peter Rehling

Open access · bronzeAbstract read
In one paragraph

Article in Molecular and cellular biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.6field-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

21 citing papers in PubMed, 45 citations in OpenAlex.

  1. Subcellular localization as a driver of protein function.Nature reviews. Molecular cell biology · 2026
    Review
  2. Review
  3. Mitochondrial dysfunction: mechanisms and advances in therapy.Signal transduction and targeted therapy · 2024
    Review
  4. Article
  5. In Vitro Transcriptional Response ofInternational journal of molecular sciences · 2023
    Article
  6. Review
  7. Article
  8. Article
  9. Review
  10. Article
  11. Review
  12. Article
  13. Article
  14. The mitochondrial gate reveals its secrets.Nature structural & molecular biology · 2019
    Article
  15. Transport of Proteins into Mitochondria.The protein journal · 2019
    Review
  16. Mitochondrial proteins: from biogenesis to functional networks.Nature reviews. Molecular cell biology · 2019
    Review
  17. Article
  18. Review
  19. Article
  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 at 4 institutions in 2 countries.

Jonathan MelinInstitute of Cellular Biochemistry, University Medical Center Göttingen, Göttingen, Germany.
Christian SchulzInstitute of Cellular Biochemistry, University Medical Center Göttingen, Göttingen, Germany.
Lidia WrobelInternational Institute of Molecular and Cell Biology, Warsaw, Poland.
Olaf BernhardInstitute of Cellular Biochemistry, University Medical Center Göttingen, Göttingen, Germany.
Agnieszka ChacinskaInternational Institute of Molecular and Cell Biology, Warsaw, Poland.
Olaf JahnProteomics Group, Max Planck Institute for Experimental Medicine, Göttingen, Germany.
Bernhard SchmidtInstitute of Cellular Biochemistry, University Medical Center Göttingen, Göttingen, Germany.
Peter RehlingInstitute of Cellular Biochemistry, University Medical Center Göttingen, Göttingen, Germany Max Planck Institute for Biophysical Chemistry, Göttingen, Germany Peter.Rehling@medizin.uni-goettingen.de.
Universitätsmedizin Göttingen · DEInternational Institute of Molecular and Cell Biology · PLMax Planck Institute of Experimental Medicine · DEUniversity of Göttingen · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

More than 70% of mitochondrial proteins utilize N-terminal presequences as targeting signals. Presequence interactions with redundant cytosolic receptor domains of the translocase of the outer mitochondrial membrane (TOM) are well established. However, after the presequence enters the protein-conducting Tom40 channel, the recognition events that occur at the trans side leading up to the engagement of the presequence with inner membrane-bound receptors are less well defined. Using a photoaffinity-labeling approach with modified presequence peptides, we identified Tom40 as a presequence interactor of the TOM complex. Utilizing mass spectrometry, we mapped Tom40's presequence-interacting regions to both sides of the β-barrel. Analysis of a phosphorylation site within one of the presequence-interacting regions revealed altered translocation kinetics along the presequence pathway. Our analyses assess the relation between the identified presequence-binding region of Tom40 and the intermembrane space domain of Tom22. The identified presequence-interacting region of Tom40 is capable of functioning independently of the established trans-acting TOM presequence-binding domain during matrix import.

Indexed as

Protein TransportAnimalsBinding SitesCarrier ProteinsMass SpectrometryMitochondriaMitochondrial Membrane Transport ProteinsMitochondrial Precursor Protein Import Complex ProteinsMutationPhosphorylationProtein ConformationProtein PrecursorsProtein Structure, SecondarySaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsStructural Homology, ProteinCarrier ProteinsMitochondrial Membrane Transport ProteinsMitochondrial Precursor Protein Import Complex ProteinsProtein PrecursorsSaccharomyces cerevisiae ProteinsTOM22 protein, S cerevisiaeTom40 protein, S cerevisiae

Identifiers

PMID25002531
PMCPMC4135617
OpenAlexW2104456628

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.