Evidence map›Paper›PMID 40047641›Full record

ArticleThe Journal of cell biology2025

Cytoplasmic ribosomes on mitochondria alter the local membrane environment for protein import.

Ya-Ting Chang, Benjamin A Barad, Juliette Hamid, Hamidreza Rahmani, Brian M Zid, Danielle A Grotjahn

Abstract read
In one paragraph

Article in The Journal of cell biology, 2025. 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
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  8. Quality control of protein import into mammalian mitochondria.Protein science : a publication of the Protein Society · 2026
    Review
  9. Article
  10. Article
  11. Article
  12. Review
  13. Review
  14. Article
  15. Cytoplasmic ribosomes hitchhike on mitochondria to dendrites.bioRxiv : the preprint server for biology · 2024
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors.

Ya-Ting ChangDepartment of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA, USA.ORCID 0000-0003-2580-4622
Benjamin A BaradDepartment of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA, USA.ORCID 0000-0002-1016-862X
Juliette HamidDepartment of Chemistry and Biochemistry, University of California San Diego, La Jolla, CA, USA.ORCID 0009-0007-3560-6976
Hamidreza RahmaniDepartment of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA, USA.ORCID 0000-0003-0222-6989
Brian M ZidDepartment of Chemistry and Biochemistry, University of California San Diego, La Jolla, CA, USA.ORCID 0000-0003-1876-2479
Danielle A GrotjahnDepartment of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA, USA.ORCID 0000-0001-5908-7882

Funding

Defining Endoplasmic Reticulum Stress-Development Mitochondria RemodelingRF1NS125674 · NINDS · SCRIPPS RESEARCH INSTITUTE, THE · PI WISEMAN, ROCKLAND LUKE · 2022 to 2022
$2.4M
Undergraduate Summer Research Supplement to R35R35GM128798 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI ZID, BRIAN MATTHEW · 2018 to 2023
$2.3M
Defining Endoplasmic Reticulum Stress-Development Mitochondria RemodelingR01NS125674 · NINDS · SCRIPPS RESEARCH INSTITUTE, THE · PI Rockland Luke Wiseman · 2025 to 2026
$1.4M
High-speed direct detector for cryo electron microscopyS10OD032467 · OD · SCRIPPS RESEARCH INSTITUTE, THE · PI LANDER, GABRIEL C · 2022 to 2022
$600k
Damon Runyon Cancer Research Foundation DRR-65-21NIGMS NIH HHS R35 GM128798NIH HHS RF1NS125674NIH HHS S10 OD032467NINDS NIH HHS R01 NS125674NINDS NIH HHS RF1 NS125674
6 · The paper itself

Abstract

Most of the mitochondria proteome is nuclear-encoded, synthesized by cytoplasmic ribosomes, and targeted to the mitochondria posttranslationally. However, a subset of mitochondrial-targeted proteins is imported co-translationally, although the molecular mechanisms governing this process remain unclear. We employ cellular cryo-electron tomography to visualize interactions between cytoplasmic ribosomes and mitochondria in Saccharomyces cerevisiae. We use surface morphometrics tools to identify a subset of ribosomes optimally oriented on mitochondrial membranes for protein import. This allows us to establish the first subtomogram average structure of a cytoplasmic ribosome at the mitochondrial surface in the native cellular context, which showed three distinct connections with the outer mitochondrial membrane surrounding the peptide exit tunnel. Further, this analysis demonstrated that cytoplasmic ribosomes primed for mitochondrial protein import cluster on the outer mitochondrial membrane at sites of local constrictions of the outer and inner mitochondrial membranes. Overall, our study reveals the architecture and the spatial organization of cytoplasmic ribosomes at the mitochondrial surface, providing a native cellular context to define the mechanisms that mediate efficient mitochondrial co-translational protein import.

Indexed as

CytoplasmMitochondriaMitochondrial MembranesMitochondrial ProteinsRibosomesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsProtein TransportMitochondrial ProteinsSaccharomyces cerevisiae Proteins

Identifiers

PMID40047641
PMCPMC11893167

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Registered trials

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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.