Evidence map›Paper›PMID 36704946›Full record

ArticleThe EMBO journal2023

MitoStores: chaperone-controlled protein granules store mitochondrial precursors in the cytosol.

Lena Krämer, Niko Dalheimer, Markus Räschle, Zuzana Storchová, Jan Pielage, Felix Boos, Johannes M Herrmann

Open access · hybridAbstract read
In one paragraph

Article in The EMBO journal, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
13.1field-weighted citation impact, top 1% 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

44 citing papers in PubMed, 79 citations in OpenAlex.

  1. More than the 'master regulator of cytosolic proteostasis': new roles for HSF1 in promoting tissue health.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2026
    Review
  2. Review
  3. Article
  4. Mass spectrometry proteomics for studying mitostasis.Protein science : a publication of the Protein Society · 2026
    Review
  5. Review
  6. Dynamic disorder is crucial for mitochondrial protein import.Protein science : a publication of the Protein Society · 2026
    Review
  7. The role of the nucleus in the control of mitochondrial precursor proteins in yeast.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. mtHsp70 chaperone converts mitochondrial proteostasis stress into impaired protein import.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  10. Article
  11. Functions of J-domain proteins in mitochondrial protein biogenesis.Protein science : a publication of the Protein Society · 2026
    Review
  12. Mitochondrial presequences are more than just address labels.Protein science : a publication of the Protein Society · 2026
    Review
  13. Article
  14. Review
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors at 1 institution in 1 country.

Lena KrämerCell Biology, University of Kaiserslautern, Kaiserslautern, Germany.
Niko DalheimerCell Biology, University of Kaiserslautern, Kaiserslautern, Germany.
Markus RäschleMolecular Genetics, University of Kaiserslautern, Kaiserslautern, Germany.ORCID 0000-0002-6737-7203
Zuzana StorchováMolecular Genetics, University of Kaiserslautern, Kaiserslautern, Germany.ORCID 0000-0003-2376-7047
Jan PielageZoology and Neurobiology, University of Kaiserslautern, Kaiserslautern, Germany.ORCID 0000-0002-5115-5884
Felix BoosCell Biology, University of Kaiserslautern, Kaiserslautern, Germany.
Johannes M HerrmannCell Biology, University of Kaiserslautern, Kaiserslautern, Germany.ORCID 0000-0003-2081-4506
University of Kaiserslautern · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Hundreds of nucleus-encoded mitochondrial precursor proteins are synthesized in the cytosol and imported into mitochondria in a post-translational manner. However, the early processes associated with mitochondrial protein targeting remain poorly understood. Here, we show that in Saccharomyces cerevisiae, the cytosol has the capacity to transiently store mitochondrial matrix-destined precursors in dedicated deposits that we termed MitoStores. Competitive inhibition of mitochondrial protein import via clogging of import sites greatly enhances the formation of MitoStores, but they also form during physiological cell growth on nonfermentable carbon sources. MitoStores are enriched for a specific subset of nucleus-encoded mitochondrial proteins, in particular those containing N-terminal mitochondrial targeting sequences. Our results suggest that MitoStore formation suppresses the toxic potential of aberrantly accumulating mitochondrial precursor proteins and is controlled by the heat shock proteins Hsp42 and Hsp104. Thus, the cytosolic protein quality control system plays an active role during the early stages of mitochondrial protein targeting through the coordinated and localized sequestration of mitochondrial precursor proteins.

Indexed as

Molecular ChaperonesSaccharomyces cerevisiae ProteinsCytosolHeat-Shock ProteinsMitochondriaMitochondrial ProteinsProtein TransportSaccharomyces cerevisiaeHeat-Shock ProteinsHsP104 protein, S cerevisiaeHSP42 protein, S cerevisiaeMitochondrial ProteinsMolecular ChaperonesSaccharomyces cerevisiae Proteinschaperonesmitochondriaproteasomeprotein aggregatesprotein translocation

Identifiers

PMID36704946
PMCPMC10068336
OpenAlexW4318214750

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.