Evidence map›Paper›PMID 24705649›Full record

ArticleNucleic acids research2014

Structural basis for binding the TREX2 complex to nuclear pores, GAL1 localisation and mRNA export.

Divyang Jani, Eugene Valkov, Murray Stewart

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.

0numbers the graph read from it
0cells of the map it votes in
55citing papers in PubMed
3.0field-weighted citation impact, top 8% 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

55 citing papers in PubMed, 81 citations in OpenAlex.

  1. Sus1 Modulates Chromatin Remodeling and Gene Expression via the Cell Wall Integrity Pathway in Saccharomyces cerevisiae.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2026
    Article
  2. Structure, function and assembly of nuclear pore complexes.Nature reviews. Molecular cell biology · 2026
    Review
  3. Viral interference of nucleocytoplasmic transport.The Journal of biological chemistry · 2025
    Review
  4. Review
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  6. Article
  7. Review
  8. Identification of divergentbioRxiv : the preprint server for biology · 2025
    Article
  9. Article
  10. Article
  11. Structures and mRNP remodeling mechanism of the TREX-2 complex.Structure (London, England : 1993) · 2025
    Article
  12. 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

3 authors at 1 institution in 1 country.

Divyang JaniMRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge Biomedical Campus, Cambridge, CB2 0QH, UK.
Eugene ValkovMRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge Biomedical Campus, Cambridge, CB2 0QH, UK.
Murray StewartMRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge Biomedical Campus, Cambridge, CB2 0QH, UK ms@mrc-lmb.cam.ac.uk.
MRC Laboratory of Molecular Biology · GB

Funding

Medical Research Council MC_U105178939Medical Research Council U105178939Wellcome Trust 080522
6 · The paper itself

Abstract

The conserved Sac3:Thp1:Sem1:Sus1:Cdc31 (TREX2) complex binds to nuclear pore complexes (NPCs) and, in addition to integrating mRNA nuclear export with preceding steps in the gene expression pathway, facilitates re-positioning of highly regulated actively transcribing genes (such as GAL1) to NPCs. Although TREX2 is thought to bind NPC protein Nup1, defining the precise role of this interaction has been frustrated by the complex pleiotropic phenotype exhibited by nup1Δ strains. To provide a structural framework for understanding the binding of TREX2 to NPCs and its function in the gene expression pathway, we have determined the structure of the Nup1:TREX2 interaction interface and used this information to engineer a Sac3 variant that impairs NPC binding while not compromising TREX2 assembly. This variant inhibited the NPC association of both de-repressed and activated GAL1 and also produced mRNA export and growth defects. These results indicate that the TREX2:Nup1 interaction facilitates the efficient nuclear export of bulk mRNA together with the re-positioning of GAL1 to NPCs that is required for transcriptional control that is mediated by removal of SUMO from repressors by NPC-bound Ulp1.

Indexed as

Active Transport, Cell NucleusCell NucleusGalactokinaseModels, MolecularMutationNuclear PoreNuclear Pore Complex ProteinsNuclear ProteinsNucleocytoplasmic Transport ProteinsPorinsProtein Interaction Domains and MotifsRNA-Binding ProteinsRNA, MessengerRNA TransportSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsGAL1 protein, S cerevisiaeGalactokinaseNuclear Pore Complex ProteinsNuclear ProteinsNucleocytoplasmic Transport ProteinsNUP1 protein, S cerevisiaePorinsRNA-Binding ProteinsRNA, MessengerSAC3 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSus1 protein, S cerevisiae

Identifiers

PMID24705649
PMCPMC4041426
OpenAlexW1989644696

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.