Evidence map›Paper›PMID 16000379›Full record

ArticleMolecular biology of the cell2005

Interaction between the shuttling mRNA export factor Gle1 and the nucleoporin hCG1: a conserved mechanism in the export of Hsp70 mRNA.

Frederic Kendirgi, Deborah J Rexer, Abel R Alcázar-Román, Halina M Onishko, Susan R Wente

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.

0numbers the graph read from it
0cells of the map it votes in
59citing papers in PubMed
1.8field-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

59 citing papers in PubMed, 81 citations in OpenAlex.

  1. Article
  2. Article
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  4. Review
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  7. Review
  8. Advances in the understanding of nuclear pore complexes in human diseases.Journal of cancer research and clinical oncology · 2024
    Review
  9. Article
  10. Review
  11. Unraveling docking and initiation of mRNA export through the nuclear pore complex.BioEssays : news and reviews in molecular, cellular and developmental biology · 2022
    Article
  12. Nuclear Pore Dysfunction in Neurodegeneration.Neurotherapeutics : the journal of the American Society for Experimental NeuroTherapeutics · 2022
    Review
  13. Article
  14. Article
  15. 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
  16. Review
  17. Review
  18. Article
  19. Article
  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

5 authors at 1 institution in 1 country.

Frederic KendirgiDepartment of Cell and Developmental Biology, Vanderbilt University Medical Center, Nashville, TN 37232-8240, USA.
Deborah J Rexer
Abel R Alcázar-Román
Halina M Onishko
Susan R Wente
Vanderbilt University Medical Center · US

Funding

Molecular Analysis of Nuclear Pore Complex FunctionR37GM051219 · NIGMS · VANDERBILT UNIVERSITY · PI WENTE, SUSAN R. · 2010 to 2019
$5.6M
MOLECULAR ANALYSIS OF NUCLEAR PORE COMPLEX FUNCTIONR01GM051219 · NIGMS · WASHINGTON UNIVERSITY · PI WENTE, SUSAN R. · 1994 to 2009
$4.2M
Analysis of Nuclear Pore Complex Assembly FactorsF32GM072272 · NIGMS · VANDERBILT UNIVERSITY · PI REXER, DEBORAH · 2004 to 2005
$69k
NIGMS NIH HHS F32 GM072272NIGMS NIH HHS GM072272NIGMS NIH HHS GM51219NIGMS NIH HHS R01 GM051219NIGMS NIH HHS R37 GM051219
6 · The paper itself

Abstract

Translocation of messenger RNAs through the nuclear pore complex (NPC) requires coordinated physical interactions between stable NPC components, shuttling transport factors, and mRNA-binding proteins. In budding yeast (y) and human (h) cells, Gle1 is an essential mRNA export factor. Nucleocytoplasmic shuttling of hGle1 is required for mRNA export; however, the mechanism by which hGle1 associates with the NPC is unknown. We have previously shown that the interaction of hGle1 with the nucleoporin hNup155 is necessary but not sufficient for targeting hGle1 to NPCs. Here, we report that the unique C-terminal 43 amino acid region of the hGle1B isoform mediates binding to the C-terminal non-FG region of the nucleoporin hCG1/NPL1. Moreover, hNup155, hGle1B, and hCG1 formed a heterotrimeric complex in vitro. This suggested that these two nucleoporins were required for the NPC localization of hGle1. Using an siRNA-based approach, decreased levels of hCG1 resulted in hGle1 accumulation in cytoplasmic foci. This was coincident with inhibition of heat shock-induced production of Hsp70 protein and export of the Hsp70 mRNA in HeLa cells. Because this closely parallels the role of the hCG1 orthologue yNup42/Rip1, we speculate that hGle1-hCG1 function in the mRNA export mechanism is highly conserved.

Indexed as

Biological TransportCarrier ProteinsConserved SequenceGenes, ReporterHeLa CellsHSP70 Heat-Shock ProteinsHumansNuclear Pore Complex ProteinsNuclear ProteinsNucleocytoplasmic Transport ProteinsProtein Structure, TertiaryRecombinant Fusion ProteinsRNA, MessengerTwo-Hybrid System TechniquesCarrier ProteinsGle1 protein, humanHSP70 Heat-Shock ProteinsNuclear Pore Complex ProteinsNuclear ProteinsNucleocytoplasmic Transport ProteinsNUP155 protein, humanNUP42 protein, humanRecombinant Fusion ProteinsRNA, Messenger

Identifiers

PMID16000379
PMCPMC1196339
OpenAlexW2132665334

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.