Evidence map›Paper›PMID 33191911›Full record

ArticleeLife2020

Structure of the human core transcription-export complex reveals a hub for multivalent interactions.

Thomas Pühringer, Ulrich Hohmann, Laura Fin, Belén Pacheco-Fiallos, Ulla Schellhaas, Julius Brennecke, Clemens Plaschka

Open access · goldAbstract read
In one paragraph

Article in eLife, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.

0numbers the graph read from it
0cells of the map it votes in
59citing papers in PubMed
4.0field-weighted citation impact, top 5% 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

59 citing papers in PubMed, 96 citations in OpenAlex.

  1. Article
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  10. Structure, function and assembly of nuclear pore complexes.Nature reviews. Molecular cell biology · 2026
    Review
  11. Article
  12. Article
  13. Review
  14. Viral interference of nucleocytoplasmic transport.The Journal of biological chemistry · 2025
    Review
  15. Review
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  17. Article
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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

7 authors at 2 institutions in 1 country.

Thomas Pühringer *Research Institute of Molecular Pathology (IMP), Vienna BioCenter (VBC), Vienna, Austria.ORCID 0000-0001-9127-9120
Ulrich Hohmann *Research Institute of Molecular Pathology (IMP), Vienna BioCenter (VBC), Vienna, Austria.ORCID 0000-0003-2124-1439
Laura FinResearch Institute of Molecular Pathology (IMP), Vienna BioCenter (VBC), Vienna, Austria.
Belén Pacheco-FiallosResearch Institute of Molecular Pathology (IMP), Vienna BioCenter (VBC), Vienna, Austria.
Ulla SchellhaasResearch Institute of Molecular Pathology (IMP), Vienna BioCenter (VBC), Vienna, Austria.ORCID 0000-0002-9684-9839
Julius BrenneckeInstitute of Molecular Biotechnology of the Austrian Academy of Sciences (IMBA), Vienna, Austria.
Clemens PlaschkaResearch Institute of Molecular Pathology (IMP), Vienna BioCenter (VBC), Vienna, Austria.ORCID 0000-0002-6020-9514
Research Institute of Molecular Pathology · ATInstitute of Molecular Biotechnology · AT

Funding

Austrian Science Fund F4303 and W1207H2020 European Research Council ERC-2015-CoG 682181H2020 European Research Council ERC-2020-STG 949081Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung P2GEP3_188343
6 · The paper itself

Abstract

The export of mRNA from nucleus to cytoplasm requires the conserved and essential transcription and export (TREX) complex (THO-UAP56/DDX39B-ALYREF). TREX selectively binds mRNA maturation marks and licenses mRNA for nuclear export by loading the export factor NXF1-NXT1. How TREX integrates these marks and achieves high selectivity for mature mRNA is poorly understood. Here, we report the cryo-electron microscopy structure of the human THO-UAP56/DDX39B complex at 3.3 Å resolution. The seven-subunit THO-UAP56/DDX39B complex multimerizes into a 28-subunit tetrameric assembly, suggesting that selective recognition of mature mRNA is facilitated by the simultaneous sensing of multiple, spatially distant mRNA regions and maturation marks. Two UAP56/DDX39B RNA helicases are juxtaposed at each end of the tetramer, which would allow one bivalent ALYREF protein to bridge adjacent helicases and regulate the TREX-mRNA interaction. Our structural and biochemical results suggest a conserved model for TREX complex function that depends on multivalent interactions between proteins and mRNA.

Indexed as

Models, MolecularActive Transport, Cell NucleusCryoelectron MicroscopyHumansMultiprotein ComplexesProtein ConformationRNA-Binding ProteinsRNA, MessengerRNA TransportMultiprotein ComplexesRNA-Binding ProteinsRNA, Messengerchromosomescryo-EMgene expressionhumanmacromolecular complexesmolecular biophysicsmRNA exportmRNA packagingstructural biology

Identifiers

PMID33191911
PMCPMC7744094
OpenAlexW3105080990

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.