Evidence map›Paper›PMID 7929578›Full record

ArticleThe Journal of cell biology1994

nup1 mutants exhibit pleiotropic defects in nuclear pore complex function.

A M Bogerd, J A Hoffman, D C Amberg, G R Fink, L I Davis

Abstract read
In one paragraph

Article in The Journal of cell biology, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
–field-weighted citation impact
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

47 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Shaping the nucleus: factors and forces.Journal of cellular biochemistry · 2012
    Review
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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.

A M BogerdHoward Hughes Medical Institute, Department of Genetics, Duke University Medical Center, Durham, North Carolina 27710.
J A Hoffman
D C Amberg
G R Fink
L I Davis

Funding

REGULATION OF THE METABOLISM OF EUCARYOTIC MRNAR01GM033998 · NIGMS · DARTMOUTH COLLEGE · PI COLE, CHARLES N. · 1985 to 2013
$6.1M
NIGMS NIH HHS GM 33998
6 · The paper itself

Abstract

The NUP1 gene of Saccharomyces cerevisiae encodes one member of a family of nuclear pore complex proteins (nucleoporins) conserved from yeast to vertebrates. We have used mutational analysis to investigate the function of Nup1p. Deletion of either the amino- or carboxy-terminal domain confers a lethal phenotype, but partial truncations at either end affect growth to varying extents. Amino-terminal truncation causes mislocalization and degradation of the mutant protein, suggesting that this domain is required for targeting Nup1p to the nuclear pore complex. Carboxy-terminal mutants are stable but do not have wild-type function, and confer a temperature sensitive phenotype. Both import of nuclear proteins and export of poly(A) RNA are defective at the nonpermissive temperature. In addition, nup1 mutant cells become multinucleate at all temperatures, a phenotype suggestive of a defect in nuclear migration. Tubulin staining revealed that the mitotic spindle appears to be oriented randomly with respect to the bud, in spite of the presence of apparently normal cytoplasmic microtubules connecting one spindle pole body to the bud tip. EM analysis showed that the nuclear envelope forms long projections extending into the cytoplasm, which appear to have detached from the bulk of the nucleus. Our results suggest that Nup1p may be required to retain the structural integrity between the nuclear envelope and an underlying nuclear scaffold, and that this connection is required to allow reorientation of the nucleus in response to cytoskeletal forces.

Indexed as

Nuclear Pore Complex ProteinsBase SequenceBiological TransportCell NucleusDNA Mutational AnalysisFungal ProteinsGenes, FungalMembrane ProteinsMicroscopy, ElectronMolecular Sequence DataMutagenesisNuclear EnvelopeNuclear ProteinsPhenotypeRNA, FungalRNA, MessengerFungal ProteinsMembrane ProteinsNuclear Pore Complex ProteinsNuclear ProteinsNUP1 protein, S cerevisiaeRNA, FungalRNA, MessengerTubulin

Identifiers

PMID7929578
PMCPMC2120204

What OpenQuestion holds

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LicenceCC BY-NC-SA
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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.