Evidence map›Paper›PMID 35931083›Full record

ArticleMolecular cell2022

PEX5 translocation into and out of peroxisomes drives matrix protein import.

Michael L Skowyra, Tom A Rapoport

Abstract read
In one paragraph

Article in Molecular cell, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing 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

39 citing papers in PubMed.

  1. Building peroxisomes: perspectives on plant peroxins.Biochemical Society transactions · 2026
    Review
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  7. Polyunsaturated fatty acid metabolism in the retinal pigment epithelium and its association with outer retinal disease.Mammalian genome : official journal of the International Mammalian Genome Society · 2026
    Review
  8. Article
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  10. Characterization ofJournal of fungi (Basel, Switzerland) · 2026
    Article
  11. Article
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  15. Article
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  18. Pieces of the peroxisomal import puzzle.Nature cell biology · 2025
    Article
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  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

2 authors.

Michael L SkowyraHoward Hughes Medical Institute and Department of Cell Biology, Harvard Medical School, 240 Longwood Avenue, Boston, MA 02115, USA.
Tom A RapoportHoward Hughes Medical Institute and Department of Cell Biology, Harvard Medical School, 240 Longwood Avenue, Boston, MA 02115, USA. Electronic address: tom_rapoport@hms.harvard.edu.

Funding

PROTEIN TRANSPORT INTO MAMMALIAN ENDOPLASMIC RETICULUMR01GM052586 · NIGMS · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI Tom A Rapoport · 1995 to 2026
$11.9M
Howard Hughes Medical InstituteNIGMS NIH HHS R01 GM052586
6 · The paper itself

Abstract

Peroxisomes are ubiquitous organelles whose dysfunction causes fatal human diseases. Most peroxisomal enzymes are imported from the cytosol by the receptor PEX5, which interacts with a docking complex in the peroxisomal membrane and then returns to the cytosol after monoubiquitination by a membrane-embedded ubiquitin ligase. The mechanism by which PEX5 shuttles between cytosol and peroxisomes and releases cargo inside the lumen is unclear. Here, we use Xenopus egg extract to demonstrate that PEX5 accompanies cargo completely into the lumen, utilizing WxxxF/Y motifs near its N terminus that bind a lumenal domain of the docking complex. PEX5 recycling is initiated by an amphipathic helix that binds to the lumenal side of the ubiquitin ligase. The N terminus then emerges in the cytosol for monoubiquitination. Finally, PEX5 is extracted from the lumen, resulting in the unfolding of the receptor and cargo release. Our results reveal the unique mechanism by which PEX5 ferries proteins into peroxisomes.

Indexed as

PeroxisomesReceptors, Cytoplasmic and NuclearCarrier ProteinsHumansLigasesPeroxisome-Targeting Signal 1 ReceptorProtein TransportUbiquitinCarrier ProteinsLigasesPeroxisome-Targeting Signal 1 ReceptorReceptors, Cytoplasmic and NuclearUbiquitindocking complexperoxisomePEX14PEX5protein importPTS1recyclingubiquitin ligase

Identifiers

PMID35931083
PMCPMC9444985

What OpenQuestion holds

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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.