Evidence map›Paper›PMID 8930904›Full record

ArticleMolecular biology of the cell1996

Nuclear transport defects and nuclear envelope alterations are associated with mutation of the Saccharomyces cerevisiae NPL4 gene.

C DeHoratius, P A Silver

Open access · greenAbstract 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 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
1.6field-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

35 citing papers in PubMed, 72 citations in OpenAlex.

  1. Article
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  5. Review
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  8. The ESCRT machinery: new roles at new holes.Current opinion in cell biology · 2016
    Review
  9. ESCRTs breach the nuclear border.Nucleus (Austin, Tex.) · 2015
    Article
  10. Review
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. TDP-43 mediates degeneration in a novel Drosophila model of disease caused by mutations in VCP/p97.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2010
    Article
  17. Article
  18. Article
  19. Structural insights into the p97-Ufd1-Npl4 complex.Proceedings of the National Academy of Sciences of the United States of America · 2007
    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

2 authors at 1 institution in 1 country.

C DeHoratiusDepartment of Molecular Biology, Princeton University, New Jersey 08544, USA.
P A Silver
Princeton University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

To identify components involved in nuclear protein import, we used a genetic selection to isolate mutants that mislocalized a nuclear-targeted protein. We identified temperature-sensitive mutants that accumulated several different nuclear proteins in the cytoplasm when shifted to the semipermissive temperature of 30 degrees C; these were termed npl (nuclear protein localization) mutants. We now present the properties of yeast strains bearing mutations in the NPL4 gene and report the cloning of the NPL4 gene and the characterization of the Np14 protein. The npl4-1 mutant was isolated by the previously described selection scheme. The second allele, npl4-2, was identified from an independently derived collection of temperature-sensitive mutants. The npl4-1 and npl4-2 strains accumulate nuclear-targeted proteins in the cytoplasm at the nonpermissive temperature consistent with a defect in nuclear protein import. Using an in vitro nuclear import assay, we show that nuclei prepared from temperature-shifted npl4 mutant cells are unable to import nuclear-targeted proteins, even in the presence of cytosol prepared from wild-type cells. In addition, npl4-2 cells accumulate poly(A)+ RNA in the nucleus at the nonpermissive temperature, consistent with a failure to export mRNA from the nucleus. The npl4-1 and npl4-2 cells also exhibit distinct, temperature-sensitive structural defects: npl4-1 cells project extra nuclear envelope into the cytoplasm, whereas npl4-2 cells from nuclear envelope herniations that appear to be filled with poly(A)+ RNA. The NPL4 gene encodes an essential M(r) 64,000 protein that is located at the nuclear periphery and localizes in a pattern similar to nuclear pore complex proteins. Taken together, these results indicate that this gene encodes a novel nuclear pore complex or nuclear pore complex-associated component required for nuclear membrane integrity and nuclear transport.

Indexed as

Genes, FungalNuclear Pore Complex ProteinsSaccharomyces cerevisiae ProteinsAmino Acid SequenceBiological TransportCell NucleusCloning, MolecularMicroscopy, ElectronMolecular Sequence DataMutationNuclear EnvelopeNuclear ProteinsNucleocytoplasmic Transport ProteinsRNA, MessengerSaccharomyces cerevisiaeTemperatureNPL4 protein, S cerevisiaeNuclear Pore Complex ProteinsNuclear ProteinsNucleocytoplasmic Transport ProteinsRNA, MessengerSaccharomyces cerevisiae Proteins

Identifiers

PMID8930904
PMCPMC276030
OpenAlexW1983341038

What OpenQuestion holds

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Read underepoch 390

Registered trials

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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.