Evidence map›Paper›PMID 24315374›Full record

ArticleCell metabolism2013

Stress-regulated translational attenuation adapts mitochondrial protein import through Tim17A degradation.

T Kelly Rainbolt, Neli Atanassova, Joseph C Genereux, R Luke Wiseman

Open access · bronzeAbstract read
In one paragraph

Article in Cell metabolism, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 120 papers.

0numbers the graph read from it
0cells of the map it votes in
120citing papers in PubMed
4.3field-weighted citation impact, top 5% 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

120 citing papers in PubMed, 195 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. Review
  3. Review
  4. Mitochondrial membrane remodeling in stress adaptation: Lipid control of organelle quality.Protein science : a publication of the Protein Society · 2026
    Review
  5. Mass spectrometry proteomics for studying mitostasis.Protein science : a publication of the Protein Society · 2026
    Review
  6. Article
  7. Proteolytic control of mitochondrial protein translocases.Protein science : a publication of the Protein Society · 2026
    Review
  8. Quality control of protein import into mammalian mitochondria.Protein science : a publication of the Protein Society · 2026
    Review
  9. Article
  10. Function and regulation of the mitochondrial stress response.Nature structural & molecular biology · 2026
    Review
  11. Article
  12. Molecular mechanisms of mitochondrial AAA+ proteases.The Journal of biological chemistry · 2026
    Review
  13. Review
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. Article

60 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

4 authors at 1 institution in 1 country.

T Kelly RainboltDepartment of Molecular & Experimental Medicine, Department of Chemical Physiology, The Scripps Research Institute, La Jolla, CA 92037, USA.
Neli Atanassova
Joseph C Genereux
R Luke Wiseman
Scripps Research Institute · US

Funding

Sensing Protein Folding Capacity in the Cell During AgingRC2AG036634 · NIA · SCRIPPS RESEARCH INSTITUTE, THE · PI BALCH, WILLIAM EDWARD, DILLIN, ANDREW G · 2009 to 2010
$1.1M
NIA NIH HHS R01 AG036634NIA NIH HHS RC2 AG036634
6 · The paper itself

Abstract

Stress-regulated signaling pathways protect mitochondrial proteostasis and function from pathologic insults. Despite the importance of stress-regulated signaling pathways in mitochondrial proteome maintenance, the molecular mechanisms by which these pathways maintain mitochondrial proteostasis remain largely unknown. We identify Tim17A as a stress-regulated subunit of the translocase of the inner membrane 23 (TIM23) mitochondrial protein import complex. We show that Tim17A protein levels are decreased downstream of stress-regulated translational attenuation induced by eukaryotic initiation factor 2α (eIF2α) phosphorylation through a mechanism dependent on the mitochondrial protease YME1L. Furthermore, we demonstrate that decreasing Tim17A attenuates TIM23-dependent protein import, promotes the induction of mitochondrial unfolded protein response (UPR)-associated proteostasis genes, and confers stress resistance in C. elegans and mammalian cells. Thus, our results indicate that Tim17A degradation is a stress-responsive mechanism by which cells adapt mitochondrial protein import efficiency and promote mitochondrial proteostasis in response to the numerous pathologic insults that induce stress-regulated translation attenuation.

Indexed as

Oxidative StressAnimalsArsenicATPases Associated with Diverse Cellular ActivitiesCaenorhabditis elegansCell LineEukaryotic Initiation Factor-2HEK293 CellsHeLa CellsHumansMetalloendopeptidasesMiceMitochondriaMitochondrial Membrane Transport ProteinsMitochondrial Precursor Protein Import Complex ProteinsMitochondrial ProteinsArsenicATPases Associated with Diverse Cellular ActivitiesEukaryotic Initiation Factor-2MetalloendopeptidasesMitochondrial Membrane Transport ProteinsMitochondrial Precursor Protein Import Complex ProteinsMitochondrial ProteinsParaquatTIMM17A protein, humanTIMM23 protein, humanYME1L1 protein, human

Identifiers

PMID24315374
PMCPMC3904643
OpenAlexW1992898664

What OpenQuestion holds

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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.