Evidence map›Paper›PMID 29382700›Full record

ArticleThe Journal of cell biology2018

Tom70 enhances mitochondrial preprotein import efficiency by binding to internal targeting sequences.

Sandra Backes, Steffen Hess, Felix Boos, Michael W Woellhaf, Sabrina Gödel, Martin Jung, Timo Mühlhaus, Johannes M Herrmann

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 104 papers.

0numbers the graph read from it
0cells of the map it votes in
104citing papers in PubMed
8.0field-weighted citation impact, top 2% 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

104 citing papers in PubMed, 170 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Dynamic disorder is crucial for mitochondrial protein import.Protein science : a publication of the Protein Society · 2026
    Review
  6. The role of the nucleus in the control of mitochondrial precursor proteins in yeast.Protein science : a publication of the Protein Society · 2026
    Review
  7. Review
  8. TDP-43: [GU]-ardian of the transcriptome.Molecular neurodegeneration · 2026
    Review
  9. Article
  10. Article
  11. Review
  12. Article
  13. From the cytosol to the inner membrane: biogenesis of the mitochondrial carrier family.Protein science : a publication of the Protein Society · 2026
    Review
  14. Article
  15. Mitochondrial presequences are more than just address labels.Protein science : a publication of the Protein Society · 2026
    Review
  16. Article
  17. A dynamic displacement mechanism drives protein import into mitochondria.bioRxiv : the preprint server for biology · 2026
    Article
  18. Review
  19. Review
  20. Article

44 more citing papers are in PubMed but not listed here.

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 2 institutions in 1 country.

Sandra BackesCell Biology, University of Kaiserslautern, Kaiserslautern, Germany.ORCID 0000-0002-0032-7690
Steffen HessCell Biology, University of Kaiserslautern, Kaiserslautern, Germany.
Felix BoosCell Biology, University of Kaiserslautern, Kaiserslautern, Germany.
Michael W WoellhafCell Biology, University of Kaiserslautern, Kaiserslautern, Germany.
Sabrina GödelComputational Systems Biology, University of Kaiserslautern, Kaiserslautern, Germany.ORCID 0000-0002-5043-1357
Martin JungMedical Biochemistry, Saarland University, Homburg, Germany.ORCID 0000-0002-1482-7020
Timo MühlhausComputational Systems Biology, University of Kaiserslautern, Kaiserslautern, Germany muehlhaus@bio.uni-kl.de.ORCID 0000-0003-3925-6778
Johannes M HerrmannCell Biology, University of Kaiserslautern, Kaiserslautern, Germany hannes.herrmann@biologie.uni-kl.de.ORCID 0000-0003-2081-4506
University of Kaiserslautern · DESaarland University · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The biogenesis of mitochondria depends on the import of hundreds of preproteins. N-terminal matrix-targeting signals (MTSs) direct preproteins to the surface receptors Tom20, Tom22, and Tom70. In this study, we show that many preproteins contain additional internal MTS-like signals (iMTS-Ls) in their mature region that share the characteristic properties of presequences. These features allow the in silico prediction of iMTS-Ls. Using Atp1 as model substrate, we show that iMTS-Ls mediate the binding to Tom70 and have the potential to target the protein to mitochondria if they are presented at its N terminus. The import of preproteins with high iMTS-L content is significantly impaired in the absence of Tom70, whereas preproteins with low iMTS-L scores are less dependent on Tom70. We propose a stepping stone model according to which the Tom70-mediated interaction with internal binding sites improves the import competence of preproteins and increases the efficiency of their translocation into the mitochondrial matrix.

Indexed as

Protein Interaction Domains and MotifsProtein Sorting SignalsChaperonin 60KineticsMitochondriaMitochondrial Membrane Transport ProteinsMitochondrial Precursor Protein Import Complex ProteinsModels, BiologicalProtein BindingProtein PrecursorsProtein TransportProteomicsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsChaperonin 60HSP60 protein, S cerevisiaeMitochondrial Membrane Transport ProteinsMitochondrial Precursor Protein Import Complex ProteinsProtein PrecursorsProtein Sorting SignalsSaccharomyces cerevisiae ProteinsTOM70 protein, S cerevisiae

Identifiers

PMID29382700
PMCPMC5881500
OpenAlexW2790831776

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.