Evidence map›Paper›PMID 9121474›Full record

ArticleMolecular and cellular biology1997

Yrb2p, a Nup2p-related yeast protein, has a functional overlap with Rna1p, a yeast Ran-GTPase-activating protein.

E Noguchi, N Hayashi, N Nakashima, T Nishimoto

Abstract read
In one paragraph

Article in Molecular and cellular biology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

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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

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3 · Its place in the literature

Who cites it

24 citing papers in PubMed.

  1. Article
  2. Review
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  8. The human T-cell leukemia virus Rex protein.Frontiers in bioscience : a journal and virtual library · 2005
    Review
  9. Article
  10. Article
  11. Article
  12. Article
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  20. A member of the Ran-binding protein family, Yrb2p, is involved in nuclear protein export.Proceedings of the National Academy of Sciences of the United States of America · 1998
    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

4 authors.

E NoguchiDepartment of Molecular Biology, Graduate School of Medical Science, Kyushu University, Fukuoka, Japan.
N Hayashi
N Nakashima
T Nishimoto

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Ran-GTPase cycle is important for nucleus-cytosol exchange of macromolecules and other nuclear processes. We employed the two-hybrid method to identify proteins interacting with Ran and the Ran GTP/GDP exchange factor. Using PRP20, encoding the Ran GTP/GDP exchange factor, we identified YRB1, previously identified as a protein able to interact with human Ran GTP/GDP exchange factor RCC1 in the two-hybrid system. Using GSP1, encoding the yeast Ran, as bait, we isolated YRB2. YRB2 encodes a protein containing a Ran-binding motif similar to that found in Yrb1p and Nup2p. Yrb1p is located in the cytosol whereas Nup2p is nuclear. Similar to Yrb1p, Yrb2p bound to GTP-Gsp1p but not to GDP-Gsp1p and enhanced the GTPase-activating activity of Rna1p. However, unlike Yrb1p, Yrb2p did not inhibit the nucleotide-releasing activity of Prp20p. While overproduction of Yrb1p inhibited the growth of a mutant possessing a PRP20 mutation (srm1-1) and suppressed the rna1-1 mutation, overproduction of Yrb2p showed no effect on the growth of these mutants. Disruption of YRB2 made yeast cold sensitive and was synthetically lethal with rna1-1 but not with nup2delta. Nuclear protein import and the mRNA export were normal in strains possessing mutations of YRB2. We propose that Yrb2p is involved in the nuclear processes of the Ran-GTPase cycle which are not related to nucleus-cytosol exchange of macromolecules.

Indexed as

Saccharomyces cerevisiae ProteinsBase SequenceBiological Transport, ActiveCell NucleusCytosolDNA PrimersFungal ProteinsGenes, FungalGTPase-Activating ProteinsGTP-Binding ProteinsHumansHybridization, GeneticMacromolecular SubstancesMutationNuclear ProteinsProtein BindingDNA PrimersFungal ProteinsGTPase-Activating ProteinsGTP-Binding ProteinsMacromolecular SubstancesNuclear ProteinsProteinsran GTP-Binding ProteinRNA1 protein, S cerevisiaeRNA, FungalRNA, MessengerSaccharomyces cerevisiae ProteinsYRB2 protein, S cerevisiae

Identifiers

PMID9121474
PMCPMC232073

What OpenQuestion holds

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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.