Evidence map›Paper›PMID 19767391›Full record

ArticleThe Journal of biological chemistry2009

Roles of Tom70 in import of presequence-containing mitochondrial proteins.

Hayashi Yamamoto, Kenji Fukui, Hisashi Takahashi, Shingo Kitamura, Takuya Shiota, Kayoko Terao, Mayumi Uchida, Masatoshi Esaki, Shuh-ichi Nishikawa, Tohru Yoshihisa and 2 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.

0numbers the graph read from it
0cells of the map it votes in
63citing papers in PubMed
3.2field-weighted citation impact, top 8% 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

63 citing papers in PubMed, 118 citations in OpenAlex.

  1. Regulation of cellular proteostasis via mitochondrial protein import.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2026
    Review
  2. The role of the nucleus in the control of mitochondrial precursor proteins in yeast.Protein science : a publication of the Protein Society · 2026
    Review
  3. Review
  4. Article
  5. From the cytosol to the inner membrane: biogenesis of the mitochondrial carrier family.Protein science : a publication of the Protein Society · 2026
    Review
  6. Mitochondrial presequences are more than just address labels.Protein science : a publication of the Protein Society · 2026
    Review
  7. Article
  8. A dynamic displacement mechanism drives protein import into mitochondria.bioRxiv : the preprint server for biology · 2026
    Article
  9. Review
  10. Article
  11. Article
  12. Mitochondrial protein import stress.Nature cell biology · 2025
    Review
  13. Article
  14. Article
  15. Nascent mitochondrial proteins initiate the localized condensation of cytosolic protein aggregates on the mitochondrial surface.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  16. Article
  17. Article
  18. Review
  19. Review
  20. Mechanisms of mitochondrial respiratory adaptation.Nature reviews. Molecular cell biology · 2022
    Review

3 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

12 authors at 4 institutions in 2 countries.

Hayashi YamamotoDepartment of Chemistry, Graduate School of Science, Japan Science and Technology Agency, Research Centre for Material Science, Nagoya University, Chikusa-ku, Nagoya 464-8602, Japan.
Kenji Fukui
Hisashi Takahashi
Shingo Kitamura
Takuya Shiota
Kayoko Terao
Mayumi Uchida
Masatoshi Esaki
Shuh-ichi Nishikawa
Tohru Yoshihisa
Koji Yamano
Toshiya Endo
Nagoya University · JPJapan Science and Technology Agency · JPGraduate School USA · USMaterial Sciences (United States) · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mitochondrial protein traffic requires precise recognition of the mitochondrial targeting signals by the import receptors on the mitochondrial surface including a general import receptor Tom20 and a receptor for presequence-less proteins, Tom70. Here we took a proteome-wide approach of mitochondrial protein import in vitro to find a set of presequence-containing precursor proteins for recognition by Tom70. The presequences of the Tom70-dependent precursor proteins were recognized by Tom20, whereas their mature parts exhibited Tom70-dependent import when attached to the presequence of Tom70-independent precursor proteins. The mature parts of the Tom70-dependent precursor proteins have the propensity to aggregate, and the presence of the receptor domain of Tom70 prevents their aggregate formation. Therefore Tom70 plays the role of a docking site for not only cytosolic chaperones but also aggregate-prone substrates to maintain their solubility for efficient transfer to downstream components of the mitochondrial import machineries.

Indexed as

Electrophoresis, Gel, Two-DimensionalMitochondriaMitochondrial Membrane Transport ProteinsMitochondrial Precursor Protein Import Complex ProteinsMitochondrial ProteinsMolecular ChaperonesProtein PrecursorsProteomeRNA, FungalSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationMitochondrial Membrane Transport ProteinsMitochondrial Precursor Protein Import Complex ProteinsMitochondrial ProteinsMolecular ChaperonesProtein PrecursorsProteomeRNA, FungalSaccharomyces cerevisiae ProteinsTOM70 protein, S cerevisiae

Identifiers

PMID19767391
PMCPMC2797234
OpenAlexW2050343565

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.