Evidence map›Paper›PMID 33526660›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2021

High-resolution imaging reveals compartmentalization of mitochondrial protein synthesis in cultured human cells.

Matthew Zorkau, Christin A Albus, Rolando Berlinguer-Palmini, Zofia M A Chrzanowska-Lightowlers, Robert N Lightowlers

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing 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

35 citing papers in PubMed.

  1. Article
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  5. Review
  6. TAPT1 interacts with SUCO to maintain the homeostasis of newly synthesized proteins and brain development in mice.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  7. Article
  8. TS2CG as a Membrane Builder.Journal of chemical theory and computation · 2025
    Article
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  11. Article
  12. Review
  13. Article
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  18. The mRNA translation initiation factor eIF4G1 controls mitochondrial oxidative phosphorylation, axonal morphogenesis, and memory.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  19. Article
  20. Article
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

5 authors.

Matthew ZorkauFaculty of Medical Sciences, Newcastle University Biosciences Institute, Newcastle upon Tyne NE2 4HH, United Kingdom.ORCID 0000-0001-6541-9564
Christin A AlbusFaculty of Medical Sciences, Newcastle University Biosciences Institute, Newcastle upon Tyne NE2 4HH, United Kingdom.ORCID 0000-0002-6259-7151
Rolando Berlinguer-PalminiBioimaging Unit, Faculty of Medical Sciences, Newcastle University, Newcastle upon Tyne NE2 4HH, United Kingdom.ORCID 0000-0002-1786-496X
Zofia M A Chrzanowska-LightowlersFaculty of Medical Sciences, Newcastle University Biosciences Institute, Newcastle upon Tyne NE2 4HH, United Kingdom; zofia.chrzanowska-lightowlers@ncl.ac.uk robert.lightowlers@ncl.ac.uk.ORCID 0000-0002-0045-3152
Robert N LightowlersFaculty of Medical Sciences, Newcastle University Biosciences Institute, Newcastle upon Tyne NE2 4HH, United Kingdom; zofia.chrzanowska-lightowlers@ncl.ac.uk robert.lightowlers@ncl.ac.uk.ORCID 0000-0002-0587-9937

Funding

Wellcome TrustWellcome Trust 203105/Z/16/Z
6 · The paper itself

Abstract

Human mitochondria contain their own genome, mitochondrial DNA, that is expressed in the mitochondrial matrix. This genome encodes 13 vital polypeptides that are components of the multisubunit complexes that couple oxidative phosphorylation (OXPHOS). The inner mitochondrial membrane that houses these complexes comprises the inner boundary membrane that runs parallel to the outer membrane, infoldings that form the cristae membranes, and the cristae junctions that separate the two. It is in these cristae membranes that the OXPHOS complexes have been shown to reside in various species. The majority of the OXPHOS subunits are nuclear-encoded and must therefore be imported from the cytosol through the outer membrane at contact sites with the inner boundary membrane. As the mitochondrially encoded components are also integral members of these complexes, where does protein synthesis occur? As transcription, mRNA processing, maturation, and at least part of the mitoribosome assembly process occur at the nucleoid and the spatially juxtaposed mitochondrial RNA granules, is protein synthesis also performed at the RNA granules close to these entities, or does it occur distal to these sites? We have adapted a click chemistry-based method coupled with stimulated emission depletion nanoscopy to address these questions. We report that, in human cells in culture, within the limits of our methodology, the majority of mitochondrial protein synthesis is detected at the cristae membranes and is spatially separated from the sites of RNA processing and maturation.

Indexed as

Cell CompartmentationImaging, Three-DimensionalProtein BiosynthesisAlkynesCells, CulturedDNA, MitochondrialGlycineHumansKineticsMitochondriaMitochondrial ProteinsMitochondrial RibosomesRNA, MitochondrialSignal TransductionAlkynesDNA, MitochondrialGlycinehomopropargylglycineMitochondrial ProteinsRNA, Mitochondrialclick chemistryhuman mitochondriamitoribosomesprotein synthesis

Identifiers

PMID33526660
PMCPMC8017971

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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.