Evidence map›Paper›PMID 28146471›Full record

ArticleNature2017

Newly born peroxisomes are a hybrid of mitochondrial and ER-derived pre-peroxisomes.

Ayumu Sugiura, Sevan Mattie, Julien Prudent, Heidi M McBride

Abstract read
PubMed Publisher
In one paragraph

Article in Nature, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 224 papers.

0numbers the graph read from it
0cells of the map it votes in
224citing papers in PubMed
20.1field-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

224 citing papers in PubMed, 382 citations in OpenAlex.

  1. Article
  2. Cellular Mechanisms Enabling Mitochondria Transfer and Transplantation.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Review
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  10. The trypanosomatid dynamin-like protein associates with glycosomes.bioRxiv : the preprint server for biology · 2026
    Article
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  12. Review
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  14. Article
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164 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors at 2 institutions in 1 country.

Ayumu SugiuraMontreal Neurological Institute, McGill University, 3801 University Ave, Montreal, Quebec, H3A 2B4, Canada.
Sevan MattieMontreal Neurological Institute, McGill University, 3801 University Ave, Montreal, Quebec, H3A 2B4, Canada.
Julien PrudentMontreal Neurological Institute, McGill University, 3801 University Ave, Montreal, Quebec, H3A 2B4, Canada.
Heidi M McBrideMontreal Neurological Institute, McGill University, 3801 University Ave, Montreal, Quebec, H3A 2B4, Canada.
McGill University · CAMontreal Neurological Institute and Hospital · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Peroxisomes function together with mitochondria in a number of essential biochemical pathways, from bile acid synthesis to fatty acid oxidation. Peroxisomes grow and divide from pre-existing organelles, but can also emerge de novo in the cell. The physiological regulation of de novo peroxisome biogenesis remains unclear, and it is thought that peroxisomes emerge from the endoplasmic reticulum in both mammalian and yeast cells. However, in contrast to the yeast system, a number of integral peroxisomal membrane proteins are imported into mitochondria in mammalian cells in the absence of peroxisomes, including Pex3, Pex12, Pex13, Pex14, Pex26, PMP34 and ALDP. Overall, the mitochondrial localization of peroxisomal membrane proteins in mammalian cells has largely been considered a mis-targeting artefact in which de novo biogenesis occurs exclusively from endoplasmic reticulum-targeted peroxins. Here, in following the generation of new peroxisomes within human patient fibroblasts lacking peroxisomes, we show that the essential import receptors Pex3 and Pex14 target mitochondria, where they are selectively released into vesicular pre-peroxisomal structures. Maturation of pre-peroxisomes containing Pex3 and Pex14 requires fusion with endoplasmic reticulum-derived vesicles carrying Pex16, thereby providing full import competence. These findings demonstrate the hybrid nature of newly born peroxisomes, expanding their functional links to mitochondria.

Indexed as

Organelle BiogenesisBacterial ProteinsCell LineEndoplasmic ReticulumFibroblastsHumansIntracellular MembranesLipoproteinsLuminescent ProteinsMembrane ProteinsMitochondriaPeroxinsPeroxisomesProtein TransportRepressor ProteinsZellweger SyndromeBacterial ProteinsLipoproteinsLuminescent ProteinsMembrane ProteinsPeroxinsPEX14 protein, humanPex3 protein, humanRepressor Proteinsyellow fluorescent protein, Bacteria

Identifiers

PMID28146471
OpenAlexW2585343016

What OpenQuestion holds

Textmetadata
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.