Evidence map›Paper›PMID 36520918›Full record

ArticleScience (New York, N.Y.)2022

Protein import into peroxisomes occurs through a nuclear pore-like phase.

Yuan Gao, Michael L Skowyra, Peiqiang Feng, Tom A Rapoport

Open access · greenAbstract read
In one paragraph

Article in Science (New York, N.Y.), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing papers in PubMed
6.8field-weighted citation impact, top 2% 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

51 citing papers in PubMed, 83 citations in OpenAlex.

  1. Building peroxisomes: perspectives on plant peroxins.Biochemical Society transactions · 2026
    Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Organelles harbour pH gradients.Research square · 2026
    Article
  11. Aging impairs peroxisome biogenesis in human B cells.The journals of gerontology. Series A, Biological sciences and medical sciences · 2026
    Article
  12. Organelles harbour pH gradients.bioRxiv : the preprint server for biology · 2025
    Article
  13. Article
  14. Article
  15. Making sense of low-complexity domains: The 2025 Lasker Basic Science Award.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  16. Article
  17. Article
  18. Review
  19. Pieces of the peroxisomal import puzzle.Nature cell biology · 2025
    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

4 authors at 1 institution in 1 country.

Yuan Gao *Department of Cell Biology, Harvard Medical School, Boston, MA 02115, USA.ORCID 0000-0003-1248-1828
Michael L Skowyra *Department of Cell Biology, Harvard Medical School, Boston, MA 02115, USA.ORCID 0000-0002-1365-034X
Peiqiang FengDepartment of Cell Biology, Harvard Medical School, Boston, MA 02115, USA.ORCID 0000-0003-1371-0290
Tom A RapoportDepartment of Cell Biology, Harvard Medical School, Boston, MA 02115, USA.ORCID 0000-0001-9911-4216
Howard Hughes Medical Institute · US

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 proteins are imported from the cytosol in a folded state by the soluble receptor PEX5. How folded cargo crosses the membrane is unknown. Here, we show that peroxisomal import is similar to nuclear transport. The peroxisomal membrane protein PEX13 contains a conserved tyrosine (Y)- and glycine (G)-rich YG domain, which forms a selective phase resembling that formed by phenylalanine-glycine (FG) repeats within nuclear pores. PEX13 resides in the membrane in two orientations that oligomerize and suspend the YG meshwork within the lipid bilayer. Purified YG domains form hydrogels into which PEX5 selectively partitions, by using conserved aromatic amino acid motifs, bringing cargo along. The YG meshwork thus forms an aqueous conduit through which PEX5 delivers folded proteins into peroxisomes.

Indexed as

Membrane ProteinsNuclear PorePeroxisomesConserved SequenceGlycineHumansProtein DomainsProtein TransportTyrosineGlycineMembrane ProteinsPEX13 protein, humanTyrosine

Identifiers

PMID36520918
PMCPMC9795577
OpenAlexW4311601716

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.