Evidence map›Paper›PMID 8970155›Full record

ArticleMolecular biology of the cell1996

GLE2, a Saccharomyces cerevisiae homologue of the Schizosaccharomyces pombe export factor RAE1, is required for nuclear pore complex structure and function.

R Murphy, J L Watkins, S R Wente

Abstract read
In one paragraph

Article in Molecular biology of the cell, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 99 papers.

0numbers the graph read from it
0cells of the map it votes in
99citing papers in PubMed
4.3field-weighted citation impact, top 5% 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

99 citing papers in PubMed, 169 citations in OpenAlex.

  1. Article
  2. Article
  3. Structure and Function of the Nuclear Pore Complex.Cold Spring Harbor perspectives in biology · 2022
    Review
  4. Article
  5. Review
  6. Article
  7. Eukaryotic Ribosome assembly and Nucleocytoplasmic Transport.Methods in molecular biology (Clifton, N.J.) · 2022
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Mosaic origin of the eukaryotic kinetochore.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  14. The Structure of the Nuclear Pore Complex (An Update).Annual review of biochemistry · 2019
    Review
  15. Article
  16. Article
  17. Identification of the NovelG3 (Bethesda, Md.) · 2018
    Article
  18. Review
  19. Article
  20. Review

39 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

3 authors at 1 institution in 1 country.

R MurphyDepartment of Cell Biology and Physiology, Washington University School of Medicine, St. Louis, Missouri 63110, USA.
J L Watkins
S R Wente
Washington University in St. Louis · US

Funding

TRAINING PROGRAM IN CELLULAR AND MOLECULAR BIOLOGYT32GM007067 · NIGMS · WASHINGTON UNIVERSITY · PI TRUE-KROB, HEATHER L · 1985 to 2020
$20.4M
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
NIGMS NIH HHS 2T32GM07067-12NIGMS NIH HHS GM-51219-02
6 · The paper itself

Abstract

To identify and characterize novel factors required for nuclear transport, a genetic screen was conducted in the yeast Saccharomyces cerevisiae. Mutations that were lethal in combination with a null allele of the gene encoding the nucleoporin Nup100p were isolated using a colony-sectoring assay. Three complementation groups of gle (for GLFG lethal) mutants were identified. In this report, the characterization of GLE2 is detailed. GLE2 encodes a 40.5-kDa polypeptide with striking similarity to that of Schizosaccharomyces pombe RAE1. In indirect immunofluorescence and nuclear pore complex fractionation experiments, Gle2p was associated with nuclear pore complexes. Mutated alleles of GLE2 displayed blockage of polyadenylated RNA export; however, nuclear protein import was not apparently diminished. Immunofluorescence and thin-section electron microscopic analysis revealed that the nuclear pore complex and nuclear envelope structure was grossly perturbed in gle2 mutants. Because the clusters of herniated pore complexes appeared subsequent to the export block, the structural perturbations were likely indirect consequences of the export phenotype. Interestingly, a two-hybrid interaction was detected between Gle2p and Srp1p, the nuclear localization signal receptor, as well as Rip1p, a nuclear export signal-interacting protein. We propose that Gle2p has a novel role in mediating nuclear transport.

Indexed as

Gene Expression Regulation, FungalGTPase-Activating ProteinsNuclear Matrix-Associated ProteinsNuclear Pore Complex ProteinsNucleocytoplasmic Transport ProteinsSaccharomyces cerevisiae ProteinsSchizosaccharomyces pombe Proteinsalpha KaryopherinsAmino Acid SequenceFungal ProteinsGenes, LethalMembrane ProteinsMolecular Sequence DataMutagenesisNuclear EnvelopeNuclear Proteinsalpha KaryopherinsFungal ProteinsGLE2 protein, S cerevisiaeGTPase-Activating ProteinsMembrane ProteinsNuclear Matrix-Associated ProteinsNuclear Pore Complex ProteinsNuclear ProteinsNucleocytoplasmic Transport ProteinsNUP100 protein, S cerevisiaeNUP116 protein, S cerevisiaeNUP145 protein, S cerevisiaePeptidesPoly AProteinsrae1 protein, S pombeRNA-Binding ProteinsSaccharomyces cerevisiae ProteinsSchizosaccharomyces pombe Proteins

Identifiers

PMID8970155
PMCPMC276040
OpenAlexW1984013070

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.