Evidence map›Paper›PMID 12668658›Full record

ArticleThe Journal of cell biology2003

An essential role for hGle1 nucleocytoplasmic shuttling in mRNA export.

Frederic Kendirgi, Dianne M Barry, Eric R Griffis, Maureen A Powers, Susan R Wente

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
1.4field-weighted citation impact, top 20% 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

39 citing papers in PubMed, 59 citations in OpenAlex.

  1. Advances in the understanding of nuclear pore complexes in human diseases.Journal of cancer research and clinical oncology · 2024
    Review
  2. Article
  3. Nuclear Pore Dysfunction in Neurodegeneration.Neurotherapeutics : the journal of the American Society for Experimental NeuroTherapeutics · 2022
    Review
  4. Evolution and diversification of the nuclear pore complex.Biochemical Society transactions · 2021
    Review
  5. Review
  6. Mutation Screening of theFrontiers in neuroscience · 2021
    Article
  7. Article
  8. Article
  9. Article
  10. Identification of the NovelG3 (Bethesda, Md.) · 2018
    Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Nup42 and IPTraffic (Copenhagen, Denmark) · 2017
    Article
  17. Article
  18. Review
  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 2 institutions in 1 country.

Frederic KendirgiDepartment of Cell and Developmental Biology, Vanderbilt University Medical Center, Nashville, TN 37232-8240, USA.
Dianne M Barry
Eric R Griffis
Maureen A Powers
Susan R Wente
Vanderbilt University Medical Center · USEmory University · US

Funding

Training Program in Biochemistry, Cell and Molecular BiologyT32GM008367 · NIGMS · EMORY UNIVERSITY · PI BOISE, LAWRENCE H., CORBETT, ANITA H. · 1990 to 2019
$5.6M
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
FUNCTIONAL ANALYSIS OF VERTEBRATE NUCLEAR TRANSPORTR01GM059975 · NIGMS · EMORY UNIVERSITY · PI POWERS, MAUREEN A. · 1999 to 2009
$2.4M
NIGMS NIH HHS GM-197190NIGMS NIH HHS GM-51219NIGMS NIH HHS GM-59975NIGMS NIH HHS R01 GM051219NIGMS NIH HHS R01 GM059975NIGMS NIH HHS R37 GM051219NIGMS NIH HHS T32 GM008367NIGMS NIH HHS T32 GM08367-13
6 · The paper itself

Abstract

Gle1 is required for mRNA export in yeast and human cells. Here, we report that two human Gle1 (hGle1) isoforms are expressed in HeLa cells (hGle1A and B). The two encoded proteins are identical except for their COOH-terminal regions. hGle1A ends with a unique four-amino acid segment, whereas hGle1B has a COOH-terminal 43-amino acid span. Only hGle1B, the more abundant isoform, localizes to the nuclear envelope (NE) and pore complex. To test whether hGle1 is a dynamic shuttling transport factor, we microinjected HeLa cells with recombinant hGle1 and conducted photobleaching studies of live HeLa cells expressing EGFP-hGle1. Both strategies show that hGle1 shuttles between the nucleus and cytoplasm. An internal 39-amino acid domain is necessary and sufficient for mediating nucleocytoplasmic transport. Using a cell-permeable peptide strategy, we document a role for hGle1 shuttling in mRNA export. An hGle1 shuttling domain (SD) peptide impairs the export of both total poly(A)+ RNA and the specific dihydrofolate reductase mRNA. Coincidentally, SD peptide-treated cells show decreased endogenous hGle1 localization at the NE and reduced nucleocytoplasmic shuttling of microinjected, recombinant hGle1. These findings pinpoint the first functional motif in hGle1 and link hGle1 to the dynamic mRNA export mechanism.

Indexed as

Amino Acid SequenceBiological Transport, ActiveCarrier ProteinsCell NucleusCytoplasmGreen Fluorescent ProteinsHeLa CellsHumansKaryopherinsLuminescent ProteinsMolecular Sequence DataNuclear EnvelopeNuclear PoreNucleocytoplasmic Transport ProteinsPoly AProtein IsoformsCarrier ProteinsGle1 protein, humanGreen Fluorescent ProteinsKaryopherinsLuminescent ProteinsNucleocytoplasmic Transport ProteinsPoly AProtein IsoformsRecombinant Fusion ProteinsRibonucleoproteinsRNA, Messenger

Identifiers

PMID12668658
PMCPMC2172758
OpenAlexW2102115478

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.