Evidence map›Paper›PMID 8755533›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1996

Nucleus-associated pools of Rna1p, the Saccharomyces cerevisiae Ran/TC4 GTPse activating protein involved in nucleus/cytosol transit.

H M Traglia, J P O'Connor, K S Tung, S Dallabrida, W C Shen, A K Hopper

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing 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

7 citing papers in PubMed.

  1. Subcellular Localization of Fad1p inLife (Basel, Switzerland) · 2021
    Article
  2. Article
  3. A domain unique to plant RanGAP is responsible for its targeting to the plant nuclear rim.Proceedings of the National Academy of Sciences of the United States of America · 2001
    Article
  4. Article
  5. Article
  6. Nucleocytoplasmic transport of macromolecules.Microbiology and molecular biology reviews : MMBR · 1997
    Review
  7. 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

6 authors.

H M TragliaDepartment of Biochemistry and Molecular Biology, Pennsylvania State University College of Medicine, Hershey 17033, USA.
J P O'Connor
K S Tung
S Dallabrida
W C Shen
A K Hopper

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Rna1p is the GTPase activating enzyme for Ran/TC4, a Ras-like GTPase necessary for nuclear/cytosolic exchange. Although most wild-type Rna1p is located in the cytosol, we found that the vast majority of the mutant Rna1-1p and, under appropriate physiological conditions, a small portion of the wild-type Rna1p cofractionate with yeast nuclei. Subnuclear fractionation studies show that most of the Rna1p is tightly associated with nuclear components, and that a portion of the active protein can be solubilized by treatments that fail to solubilize inactive Rna1-1p. To learn the precise nuclear locations of the Rna1 proteins, we studied their subcellular distributions in HeLa cells. By indirect immuno-fluorescence we show that wild-type Rna1p has three subcellular locations. The majority of the protein is distributed throughout the cytosol, but a portion of the protein is nucleus-associated, located at both the cytosolic surface and within the nucleoplasm. Mutant Rna1-1p is found at the outer nuclear surface and in the cytosol. We propose that a small pool of the wild-type Rna1p is located in the nuclear interior, supporting the model that the same components of the Ran/TC4 GTPase cycle exist on both sides of the nuclear membrane.

Indexed as

Base SequenceCell FractionationCell NucleusCytosolDNA PrimersFluorescent Antibody Technique, IndirectGTPase-Activating ProteinsGTP-Binding ProteinsHeLa CellsHumansModels, BiologicalMolecular Sequence DataMutagenesis, Site-DirectedNuclear ProteinsOpen Reading FramesPolymerase Chain ReactionDNA PrimersGTPase-Activating ProteinsGTP-Binding ProteinsNuclear ProteinsProteinsran GTP-Binding Proteinras GTPase-Activating ProteinsRecombinant ProteinsRNA1 protein, S cerevisiaeSaccharomyces cerevisiae Proteins

Identifiers

PMID8755533
PMCPMC38804

What OpenQuestion holds

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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.