Evidence map›Paper›PMID 39379376›Full record

ArticleNature communications2024

Ribosomes hibernate on mitochondria during cellular stress.

Olivier Gemin, Maciej Gluc, Higor Rosa, Michael Purdy, Moritz Niemann, Yelena Peskova, Simone Mattei, Ahmad Jomaa

Abstract read
In one paragraph

Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
–field-weighted citation impact
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

15 citing papers in PubMed.

  1. Article
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  4. Review
  5. Article
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  11. Article
  12. Article
  13. Detection and Characterization of the Eukaryotic Vacant Ribosome.International journal of molecular sciences · 2025
    Review
  14. Article
  15. Review
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.

Olivier Gemin *European Molecular Biology Laboratory, Structural and Computational Biology Unit, Meyerhofstraße 1, Heidelberg, Germany.ORCID 0000-0003-3210-7876
Maciej Gluc *Department of Molecular Physiology and Biological Physics and Center for Cell and Membrane Physiology, School of Medicine, University of Virginia, Charlottesville, USA.
Higor RosaEuropean Molecular Biology Laboratory, Structural and Computational Biology Unit, Meyerhofstraße 1, Heidelberg, Germany.ORCID 0000-0002-5743-4745
Michael PurdyDepartment of Molecular Physiology and Biological Physics and Center for Cell and Membrane Physiology, School of Medicine, University of Virginia, Charlottesville, USA.ORCID 0000-0003-0189-933X
Moritz NiemannEuropean Molecular Biology Laboratory, Structural and Computational Biology Unit, Meyerhofstraße 1, Heidelberg, Germany.ORCID 0000-0002-3351-9234
Yelena PeskovaDepartment of Molecular Physiology and Biological Physics and Center for Cell and Membrane Physiology, School of Medicine, University of Virginia, Charlottesville, USA.
Simone MatteiEuropean Molecular Biology Laboratory, Structural and Computational Biology Unit, Meyerhofstraße 1, Heidelberg, Germany. simone.mattei@embl.de.ORCID 0000-0002-2005-8977
Ahmad JomaaDepartment of Molecular Physiology and Biological Physics and Center for Cell and Membrane Physiology, School of Medicine, University of Virginia, Charlottesville, USA. ahmadjomaa@virginia.edu.ORCID 0000-0002-5543-7942

Funding

Women's Oncology Program - WONP30CA044579 · NCI · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI Dina Gould Halme · 1987 to 2026
$72.1M
NCI NIH HHS P30 CA044579
6 · The paper itself

Abstract

Cell survival under nutrient-deprived conditions relies on cells' ability to adapt their organelles and rewire their metabolic pathways. In yeast, glucose depletion induces a stress response mediated by mitochondrial fragmentation and sequestration of cytosolic ribosomes on mitochondria. This cellular adaptation promotes survival under harsh environmental conditions; however, the underlying mechanism of this response remains unknown. Here, we demonstrate that upon glucose depletion protein synthesis is halted. Cryo-electron microscopy structure of the ribosomes show that they are devoid of both tRNA and mRNA, and a subset of the particles depicted a conformational change in rRNA H69 that could prevent tRNA binding. Our in situ structural analyses reveal that the hibernating ribosomes tether to fragmented mitochondria and establish eukaryotic-specific, higher-order storage structures by assembling into oligomeric arrays on the mitochondrial surface. Notably, we show that hibernating ribosomes exclusively bind to the outer mitochondrial membrane via the small ribosomal subunit during cellular stress. We identify the ribosomal protein Cpc2/RACK1 as the molecule mediating ribosomal tethering to mitochondria. This study unveils the molecular mechanism connecting mitochondrial stress with the shutdown of protein synthesis and broadens our understanding of cellular responses to nutrient scarcity and cell quiescence.

Indexed as

MitochondriaRibosomesSchizosaccharomycesStress, PhysiologicalCytosolGlucoseModels, MolecularMolecular ConformationReceptors for Activated C KinaseSaccharomyces cerevisiaeSchizosaccharomyces pombe Proteinscpc2 protein, S pombeGlucoseReceptors for Activated C KinaseSchizosaccharomyces pombe Proteins

Identifiers

PMID39379376
PMCPMC11461667

What OpenQuestion holds

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LicenceCC BY-NC-ND
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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.