Evidence map›Paper›PMID 25452301›Full record

ArticleMolecular and cellular biology2015

Disruption of the ran system by cysteine oxidation of the nucleotide exchange factor RCC1.

Mandovi Chatterjee, Bryce M Paschal

Open access · bronzeAbstract read
In one paragraph

Article in Molecular and cellular biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
0.4field-weighted citation impact, top 37% 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

12 citing papers in PubMed, 22 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Comparative Proteomics Analysis Reveals Unique Early Signaling Response ofInternational journal of molecular sciences · 2020
    Article
  6. Article
  7. Review
  8. Mining for protein S-sulfenylation inProceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  9. Article
  10. Survive or thrive: tradeoff strategy for cellular senescence.Experimental & molecular medicine · 2017
    Review
  11. Dependence of the structure and mechanics of metaphase chromosomes on oxidized cysteines.Chromosome research : an international journal on the molecular, supramolecular and evolutionary aspects of chromosome biology · 2016
    Article
  12. Review
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.

Mandovi ChatterjeeCenter for Cell Signaling, University of Virginia, Charlottesville, Virginia Department of Cell Biology, University of Virginia, Charlottesville, Virginia.
Bryce M PaschalCenter for Cell Signaling, University of Virginia, Charlottesville, Virginia Department of Biochemistry and Molecular Genetics, University of Virginia, Charlottesville, Virginia paschal@virginia.edu.
University of Virginia · US

Funding

Regulation of nuclear transport in diseaseR01AG040162 · NIA · UNIVERSITY OF VIRGINIA · PI PASCHAL, BRYCE · 2012 to 2016
$1.6M
NIA NIH HHS 1R01AG040162NIA NIH HHS R01 AG040162
6 · The paper itself

Abstract

Transport regulation by the Ran GTPase requires its nuclear localization and GTP loading by the chromatin-associated exchange factor RCC1. These reactions generate Ran protein and Ran nucleotide gradients between the nucleus and the cytoplasm. Cellular stress disrupts the Ran gradients, but the specific mechanisms underlying this disruption have not been elucidated. We used biochemical approaches to determine how oxidative stress disrupts the Ran system. RCC1 exchange activity was reduced by diamide-induced oxidative stress and restored with dithiothreitol. Using mass spectrometry, we found that multiple solvent-exposed cysteines in RCC1 are oxidized in cells treated with diamide. The cysteines oxidized in RCC1 included Cys93, which is solvent exposed and unique because it becomes buried upon contact with Ran. A Cys93Ser substitution dramatically reduced exchange activity through an effect on RCC1 binding to RanGDP. Diamide treatment reduced the size of the mobile fraction of RCC1-green fluorescent protein in cells and inhibited nuclear import in digitonin-permeabilized cell assays. The Ran protein gradient was also disrupted by UV-induced stress but without affecting RCC1 exchange activity. Our data suggest that stress can disrupt the Ran gradients through RCC1-dependent and RCC1-independent mechanisms, possibly dependent on the particular stress condition.

Indexed as

Biological TransportCell Cycle ProteinsCell NucleusCysteineGuanine Nucleotide Exchange FactorsHumansNuclear ProteinsOxidation-ReductionOxidative StressProtein Bindingran GTP-Binding ProteinCell Cycle ProteinsCysteineGuanine Nucleotide Exchange FactorsNuclear Proteinsran GTP-Binding ProteinRCC1 protein, human

Identifiers

PMID25452301
PMCPMC4285427
OpenAlexW1982161521

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.