Evidence map›Paper›PMID 11739738›Full record

ArticleMolecular and cellular biology2002

Formation of Tap/NXT1 heterodimers activates Tap-dependent nuclear mRNA export by enhancing recruitment to nuclear pore complexes.

Heather L Wiegand, Glen A Coburn, Yan Zeng, Yibin Kang, Hal P Bogerd, Bryan R Cullen

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 66 papers.

0numbers the graph read from it
0cells of the map it votes in
66citing papers in PubMed
5.3field-weighted citation impact, top 3% 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

66 citing papers in PubMed, 124 citations in OpenAlex.

  1. Article
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  8. Unraveling docking and initiation of mRNA export through the nuclear pore complex.BioEssays : news and reviews in molecular, cellular and developmental biology · 2022
    Article
  9. Distinct roles of nuclear basket proteins in directing the passage of mRNA through the nuclear pore.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Subcellular Localization of HIV-1Journal of virology · 2017
    Article
  18. Article
  19. Article
  20. Article

6 more citing papers are in PubMed but not listed here.

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

6 authors at 3 institutions in 1 country.

Heather L WiegandHoward Hughes Medical Institute and Department of Genetics, Duke University Medical Center, Durham, North Carolina 27710, USA.
Glen A Coburn
Yan Zeng
Yibin Kang
Hal P Bogerd
Bryan R Cullen
Duke Medical Center · USDuke University Hospital · USHoward Hughes Medical Institute · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Tap protein has been shown to activate the nuclear export of mRNA species bearing retroviral constitutive transport elements and is also believed to play an essential role in the sequence nonspecific export of cellular mRNAs. However, it has remained unclear how Tap activity is regulated in vivo. Here, we report that the small NXT1/p15-1 protein functions as a critical cofactor for Tap-mediated mRNA export in both human and invertebrate cells. In the absence of NXT1 binding, the Tap protein is unable to effectively interact with components of the nuclear pore complex and both Tap nucleocytoplasmic shuttling and the nuclear export of mRNA molecules tethered to Tap are therefore severely attenuated. Formation of a Tap/NXT1 heterodimer enhances nucleoporin binding both in vitro and in vivo and induces the formation of a Tap/NXT1/nucleoporin ternary complex that is likely to be a key intermediate in the process of nuclear mRNA export. The critical importance of NXT1 for the nuclear export of poly(A)(+) RNA is emphasized by the finding that specific inhibition of the expression of the Drosophila homolog of human NXT1, by using RNA interference, results in the nuclear accumulation of poly(A)(+) RNA in cultured insect cells. These data suggest that NXT1 may act as a molecular switch that regulates the ability of Tap to mediate nuclear mRNA export by controlling the interaction of Tap with components of the nuclear pore.

Indexed as

Nucleocytoplasmic Transport ProteinsReceptors, Cytoplasmic and NuclearActive Transport, Cell NucleusAnimalsCarrier ProteinsCell LineCell NucleusCytoplasmDimerizationDrosophilaDrosophila ProteinsExportin 1 ProteinFluorescent DyesGenes, ReporterHumansKaryopherinsCarrier ProteinsDrosophila ProteinsExportin 1 ProteinFluorescent DyesKaryopherinsNuclear Pore Complex ProteinsNuclear ProteinsNucleocytoplasmic Transport ProteinsNXF1 protein, humanNxt1 protein, DrosophilaNXT1 protein, humanReceptors, CCR5Receptors, Cytoplasmic and NuclearRecombinant Fusion ProteinsRNA-Binding ProteinsRNA, Messenger

Identifiers

PMID11739738
PMCPMC134221
OpenAlexW2123459040

What OpenQuestion holds

Textmetadata
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.