Evidence map›Paper›PMID 29748336›Full record

ArticleThe Journal of cell biology2018

Xpo7 is a broad-spectrum exportin and a nuclear import receptor.

Metin Aksu, Tino Pleiner, Samir Karaca, Christin Kappert, Heinz-Jürgen Dehne, Katharina Seibel, Henning Urlaub, Markus T Bohnsack, Dirk Görlich

Open access · hybridAbstract read
In one paragraph

Article in The Journal of cell biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
2.5field-weighted citation impact, top 10% 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

38 citing papers in PubMed, 65 citations in OpenAlex.

  1. Article
  2. Article
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  4. Article
  5. A Deep-Learning Atlas of XPO1-Mediated Nuclear Export at Proteome Scale.bioRxiv : the preprint server for biology · 2026
    Article
  6. Structure, function and assembly of nuclear pore complexes.Nature reviews. Molecular cell biology · 2026
    Review
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Review
  15. Review
  16. Nuclear transport proteins: structure, function, and disease relevance.Signal transduction and targeted therapy · 2023
    Review
  17. Article
  18. Article
  19. Review
  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

9 authors at 2 institutions in 1 country.

Metin AksuDepartment of Cellular Logistics, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.ORCID 0000-0001-8627-7526
Tino PleinerDepartment of Cellular Logistics, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.ORCID 0000-0002-5104-0315
Samir KaracaBioanalytical Mass Spectrometry Group, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.
Christin KappertDepartment of Cellular Logistics, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.ORCID 0000-0003-2313-1225
Heinz-Jürgen DehneDepartment of Cellular Logistics, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.
Katharina SeibelDepartment of Cellular Logistics, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.ORCID 0000-0002-5162-0344
Henning UrlaubBioanalytical Mass Spectrometry Group, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.
Markus T BohnsackInstitute for Molecular Biology, University Medical Center Göttingen, Göttingen, Germany.ORCID 0000-0001-7063-5456
Dirk GörlichDepartment of Cellular Logistics, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany goerlich@mpibpc.mpg.de.ORCID 0000-0002-4343-5210
Max Planck Institute for Biophysical Chemistry · DEUniversitätsmedizin Göttingen · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Exportins bind cargo molecules in a RanGTP-dependent manner inside nuclei and transport them through nuclear pores to the cytoplasm. CRM1/Xpo1 is the best-characterized exportin because specific inhibitors such as leptomycin B allow straightforward cargo validations in vivo. The analysis of other exportins lagged far behind, foremost because no such inhibitors had been available for them. In this study, we explored the cargo spectrum of exportin 7/Xpo7 in depth and identified not only ∼200 potential export cargoes but also, surprisingly, ∼30 nuclear import substrates. Moreover, we developed anti-Xpo7 nanobodies that acutely block Xpo7 function when transfected into cultured cells. The inhibition is pathway specific, mislocalizes export cargoes of Xpo7 to the nucleus and import substrates to the cytoplasm, and allowed validation of numerous tested cargo candidates. This establishes Xpo7 as a broad-spectrum bidirectional transporter and paves the way for a much deeper analysis of exportin and importin function in the future.

Indexed as

Active Transport, Cell NucleusAnimalsCamelids, New WorldCell NucleusExportin 1 ProteinHeLa CellsHumansKaryopherinsNuclear PoreOocytesran GTP-Binding ProteinReceptors, Cytoplasmic and NuclearSingle-Domain AntibodiesXenopus laevisExportin 1 ProteinKaryopherinsran GTP-Binding ProteinReceptors, Cytoplasmic and NuclearSingle-Domain AntibodiesXPO7 protein, human

Identifiers

PMID29748336
PMCPMC6028547
OpenAlexW2802291077

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.