Evidence map›Paper›PMID 12384575›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2002

Karyopherin beta 2B participates in mRNA export from the nucleus.

Monee K Shamsher, Jonathan Ploski, Aurelian Radu

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

16 citing papers in PubMed, 30 citations in OpenAlex.

  1. Nuclear transport proteins: structure, function, and disease relevance.Signal transduction and targeted therapy · 2023
    Review
  2. Review
  3. Review
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Importins and exportins in cellular differentiation.Journal of cellular and molecular medicine · 2008
    Review
  10. Article
  11. Review
  12. Transportin2 functions as importin and mediates nuclear import of HuR.Proceedings of the National Academy of Sciences of the United States of America · 2004
    Article
  13. Article
  14. Review
  15. Article
  16. 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.

Monee K ShamsherThe Carl C. Icahn Institute for Gene Therapy and Molecular Medicine, Mount Sinai School of Medicine, Box 1496, 1425 Madison Avenue, New York, NY 10029, USA.
Jonathan Ploski
Aurelian Radu
Icahn School of Medicine at Mount Sinai · US

Funding

NUCLEOCYTOPLASMIC TRANSPORT--NEW FACTORS AND PATHWAYSR01GM057569 · NIGMS · MOUNT SINAI SCHOOL OF MEDICINE OF NYU · PI RADU, AURELIAN · 1998 to 2002
$577k
NIGMS NIH HHS R01 GM057569NIGMS NIH HHS R01 GM57569
6 · The paper itself

Abstract

Transport of macromolecules between the cell nucleus and cytoplasm occurs through the nuclear pores and is mediated by soluble carriers known as karyopherins (Kaps), transportins, importins, or exportins. We report that Kap beta2B (transportin-2) forms complexes with the mRNA export factor TAP in the presence of RanGTP, as shown by coimmunoprecipitation from HeLa cells. The interaction strictly depends on the presence of RanGTP. In digitonin-permeabilized cells, Kap beta2B mediates TAP-GFP export from the nuclei in the presence of RanGTP. A TAP mutant that does not coimmunoprecipitate with Kap beta2B is also not exported by Kap beta2B. In the permeabilized cells assay, TAP is also exported independently of Kap beta2B by direct interaction with nucleoporins, in agreement with previous reports. The export rate is, however, significantly lower than the Kap beta2B-mediated pathway. Both Kap beta2B and TAP are present and enriched in the poly(A)(+) RNA complexes isolated from HeLa cell nuclear lysates. Poly(A)(+) RNA strongly accumulates in the nuclei of HeLa cells treated with Kap beta2B short interfering RNA, indicating that Kap beta2B is involved in the export of at least a large proportion of the mRNA species. The export of beta-actin and GAPDH mRNA is also inhibited, whereas 28S RNA is not affected. The data support the conclusion that Kap beta2B participates directly in the export of a large proportion of cellular mRNAs, and TAP connects Kap beta2B to the mRNAs to be exported.

Indexed as

Active Transport, Cell Nucleusbeta KaryopherinsCell NucleusDown-RegulationGTPase-Activating ProteinsHeLa CellsHumansNucleocytoplasmic Transport ProteinsPoly APoly(A)-Binding ProteinsReceptors, Cytoplasmic and NuclearRNA-Binding ProteinsRNA, Messengerbeta KaryopherinsGTPase-Activating ProteinsNucleocytoplasmic Transport ProteinsNXF1 protein, humanPoly APoly(A)-Binding ProteinsRANGAP1 protein, humanReceptors, Cytoplasmic and NuclearRNA-Binding ProteinsRNA, MessengerTNPO2 protein, human

Identifiers

PMID12384575
PMCPMC137860
OpenAlexW1998551965

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.