Evidence map›Paper›PMID 25486595›Full record

ArticleeLife2014

The export receptor Crm1 forms a dimer to promote nuclear export of HIV RNA.

David S Booth, Yifan Cheng, Alan D Frankel

Open access · goldAbstract read
In one paragraph

Article in eLife, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.

0numbers the graph read from it
0cells of the map it votes in
54citing papers in PubMed
3.7field-weighted citation impact, top 6% 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

54 citing papers in PubMed, 75 citations in OpenAlex.

  1. Article
  2. Review
  3. Viral interference of nucleocytoplasmic transport.The Journal of biological chemistry · 2025
    Review
  4. Article
  5. Review
  6. Article
  7. Review
  8. Article
  9. Review
  10. Article
  11. Review
  12. Article
  13. Review
  14. Review
  15. Article
  16. Tuning Rex rules HTLV-1 pathogenesis.Frontiers in immunology · 2022
    Review
  17. Article
  18. How promising are HIV-1-based virus-like particles for medical applications.Frontiers in cellular and infection microbiology · 2022
    Review
  19. HIV Rev-isited.Open biology · 2020
    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

3 authors at 1 institution in 1 country.

David S BoothGraduate Group in Biophysics, University of California, San Francisco, San Francisco, United States.
Yifan ChengDepartment of Biochemistry and Biophysics, University of California, San Francisco, San Francisco, United States.
Alan D FrankelDepartment of Biochemistry and Biophysics, University of California, San Francisco, San Francisco, United States.
University of California, San Francisco · US

Funding

X-ray Screening and Rapid Structure DeterminationP50GM082250 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI FRANKEL, ALAN D · 2007 to 2018
$48.8M
Maximizing Opportunities for Research Excellence - Evaluation Training SupplementR25GM056847 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI DUNCAN, D'ANNE S., SELLO, JASON K · 1998 to 2023
$14.1M
STRUCTURAL BIOLOGY TRAINING PROGRAMT32GM008284 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI KORTEMME, TANJA · 1988 to 2022
$10.1M
Structural requirements for the nuclear export of HIV RNAF31GM095350 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI BOOTH, DAVID SCOTT · 2011 to 2013
$99k
NIGMS NIH HHS F31 GM095350NIGMS NIH HHS F31GM095350NIGMS NIH HHS P50 GM082250NIGMS NIH HHS P50GM088250NIGMS NIH HHS R25 GM056847NIGMS NIH HHS R25GM56847NIGMS NIH HHS T32 GM008284
6 · The paper itself

Abstract

The HIV Rev protein routes viral RNAs containing the Rev Response Element (RRE) through the Crm1 nuclear export pathway to the cytoplasm where viral proteins are expressed and genomic RNA is delivered to assembling virions. The RRE assembles a Rev oligomer that displays nuclear export sequences (NESs) for recognition by the Crm1-Ran(GTP) nuclear receptor complex. Here we provide the first view of an assembled HIV-host nuclear export complex using single-particle electron microscopy. Unexpectedly, Crm1 forms a dimer with an extensive interface that enhances association with Rev-RRE and poises NES binding sites to interact with a Rev oligomer. The interface between Crm1 monomers explains differences between Crm1 orthologs that alter nuclear export and determine cellular tropism for viral replication. The arrangement of the export complex identifies a novel binding surface to possibly target an HIV inhibitor and may point to a broader role for Crm1 dimerization in regulating host gene expression.

Indexed as

Response ElementsActive Transport, Cell NucleusBinding SitesCell Line, TumorCell NucleusCrystallography, X-RayCytosolEscherichia coliExportin 1 ProteinGene Expression RegulationHEK293 CellsHeLa CellsHIV-1Host-Pathogen InteractionsHumansKaryopherinsExportin 1 ProteinKaryopherinsran GTP-Binding ProteinReceptors, Cytoplasmic and NuclearRecombinant Proteinsrev Gene Products, Human Immunodeficiency Virusrev protein, Human Immunodeficiency Virus-1RNA, Viralbiophysicselectron microscopyHIVhumaninfectious diseasemicrobiologyRNA exportstructural biologyviruses

Identifiers

PMID25486595
PMCPMC4360530
OpenAlexW2155690286

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.