Evidence map›Paper›PMID 10846066›Full record

ArticleJournal of virology2000

Analysis of cellular factors that mediate nuclear export of RNAs bearing the Mason-Pfizer monkey virus constitutive transport element.

Y Kang, H P Bogerd, B R Cullen

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
3.3field-weighted citation impact, top 7% 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

19 citing papers in PubMed, 40 citations in OpenAlex.

  1. Virus Infection and mRNA Nuclear Export.International journal of molecular sciences · 2023
    Review
  2. Multiple nuclear-replicating viruses require the stress-induced protein ZC3H11A for efficient growth.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Karyopherin beta 2B participates in mRNA export from the nucleus.Proceedings of the National Academy of Sciences of the United States of America · 2002
    Article
  10. Article
  11. Article
  12. Article
  13. The crystal structure and mutational analysis of a novel RNA-binding domain found in the human Tap nuclear mRNA export factor.Proceedings of the National Academy of Sciences of the United States of America · 2002
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. 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 2 institutions in 1 country.

Y KangDepartment of Genetics, Duke University Medical Center, Durham, North Carolina 27710, USA.
H P Bogerd
B R Cullen
Duke University Hospital · USHoward Hughes Medical Institute · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

There is now convincing evidence that the human Tap protein plays a critical role in mediating the nuclear export of mRNAs that contain the Mason-Pfizer monkey virus constitutive transport element (CTE) and significant evidence that Tap also participates in global poly(A)(+) RNA export. Previously, we had mapped carboxy-terminal sequences in Tap that serve as an essential nucleocytoplasmic shuttling domain, while others had defined an overlapping Tap sequence that can bind to the FG repeat domains of certain nucleoporins. Here, we demonstrate that these two biological activities are functionally correlated. Specifically, mutations in Tap that block nucleoporin binding also block both nucleocytoplasmic shuttling and the Tap-dependent nuclear export of CTE-containing RNAs. In contrast, mutations that do not inhibit nucleoporin binding also fail to affect Tap shuttling. Together, these data indicate that Tap belongs to a novel class of RNA export factors that can target bound RNA molecules directly to the nuclear pore without the assistance of an importin beta-like cofactor. In addition to nucleoporins, Tap has also been proposed to interact with a cellular cofactor termed p15. Although we were able to confirm that Tap can indeed bind p15 specifically both in vivo and in vitro, a mutation in Tap that blocked p15 binding only modestly inhibited CTE-dependent nuclear RNA export. However, p15 did significantly enhance the affinity of Tap for the CTE in vitro and readily formed a ternary complex with Tap on the CTE. This result suggests that p15 may play a significant role in the recruitment of the Tap nuclear export factor to target RNA molecules in vivo.

Indexed as

KaryopherinsNuclear Pore Complex ProteinsNucleocytoplasmic Transport ProteinsReceptors, Cytoplasmic and NuclearAmino Acid SequenceAnimalsBinding SitesBiological TransportCarrier ProteinsCell LineCell Line, TransformedCell NucleusExportin 1 ProteinHeLa CellsHumansMason-Pfizer monkey virusCarrier ProteinsExportin 1 ProteinKaryopherinsNuclear Pore Complex ProteinsNuclear ProteinsNucleocytoplasmic Transport ProteinsNUP214 protein, humanNup214 protein, mouseNXF1 protein, humanNXT1 protein, humanReceptors, Cytoplasmic and NuclearRNA-Binding ProteinsRNA, Viral

Identifiers

PMID10846066
PMCPMC112081
OpenAlexW2144725211

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.