Evidence map›Paper›PMID 21173275›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2011

Dual role of the receptor Tom20 in specificity and efficiency of protein import into mitochondria.

Hayashi Yamamoto, Nobuka Itoh, Shin Kawano, Yoh-ichi Yatsukawa, Takaki Momose, Tadashi Makio, Mayumi Matsunaga, Mihoko Yokota, Masatoshi Esaki, Toshihiro Shodai and 4 more

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers.

0numbers the graph read from it
0cells of the map it votes in
65citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

65 citing papers in PubMed, 125 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Pathogens (Basel, Switzerland) · 2026
    Article
  5. Article
  6. A dynamic displacement mechanism drives protein import into mitochondria.bioRxiv : the preprint server for biology · 2026
    Article
  7. Ecm19 coordinates mitochondrial fission and cellular redox homeostasis.Redox report : communications in free radical research · 2025
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Mitochondria-containing extracellular vesicles from mouse vs. human brain endothelial cells for ischemic stroke therapy.Journal of controlled release : official journal of the Controlled Release Society · 2024
    Article
  15. Article
  16. Article
  17. Article
  18. Two conformations of the Tom20 preprotein receptor in the TOM holo complex.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  19. Article
  20. Article

5 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

14 authors at 6 institutions in 3 countries.

Hayashi YamamotoDepartment of Chemistry, Graduate School of Science, Nagoya University, Chikusa-ku, Nagoya 464-8602, Japan.
Nobuka Itoh
Shin Kawano
Yoh-ichi Yatsukawa
Takaki Momose
Tadashi Makio
Mayumi Matsunaga
Mihoko Yokota
Masatoshi Esaki
Toshihiro Shodai
Daisuke Kohda
Alyson E Aiken Hobbs
Robert E Jensen
Toshiya Endo
Nagoya University · JPJapan Science and Technology Agency · JPJohns Hopkins Medicine · USJohns Hopkins University · USKumamoto University · JPKyushu University · JP

Funding

BIOCHEMISTRY, CELLULAR AND MOLECULAR BIOLOGY PROGRAMT32GM007445 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI GREEN, RACHEL · 1985 to 2021
$24.1M
MITOCHONDRIAL DYNAMICS-MORPHOLOGY/DIVISION/SEGREGATIONR01GM054021 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI JENSEN, ROBERT E · 1996 to 2008
$2.7M
NIGMS NIH HHS 5T32GM07445NIGMS NIH HHS R01 GM054021NIGMS NIH HHS R01-GM54021NIGMS NIH HHS T32 GM007445
6 · The paper itself

Abstract

Mitochondria import most of their resident proteins from the cytosol, and the import receptor Tom20 of the outer-membrane translocator TOM40 complex plays an essential role in specificity of mitochondrial protein import. Here we analyzed the effects of Tom20 binding on NMR spectra of a long mitochondrial presequence and found that it contains two distinct Tom20-binding elements. In vitro import and cross-linking experiments revealed that, although the N-terminal Tom20-binding element is essential for targeting to mitochondria, the C-terminal element increases efficiency of protein import in the step prior to translocation across the inner membrane. Therefore Tom20 has a dual role in protein import into mitochondria: recognition of the targeting signal in the presequence and tethering the presequence to the TOM40 complex to increase import efficiency.

Indexed as

Models, MolecularBinding SitesImmunoprecipitationMitochondriaMitochondrial Membrane Transport ProteinsNuclear Magnetic Resonance, BiomolecularProtein BindingProtein TransportProton-Translocating ATPasesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsMitochondrial Membrane Transport ProteinsProton-Translocating ATPasesSaccharomyces cerevisiae ProteinsTOM20 protein, S cerevisiaeTom40 protein, S cerevisiae

Identifiers

PMID21173275
PMCPMC3017135
OpenAlexW2143191621

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.