Evidence map›Paper›PMID 27819319›Full record

ArticleScientific reports2016

Nuclear import of dimerized ribosomal protein Rps3 in complex with its chaperone Yar1.

Valentin Mitterer, Nadine Gantenbein, Ruth Birner-Gruenberger, Guillaume Murat, Helmut Bergler, Dieter Kressler, Brigitte Pertschy

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2016. 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
2.6field-weighted citation impact, top 10% 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

24 citing papers in PubMed, 31 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Ribosome Assembly and Repair.Annual review of cell and developmental biology · 2024
    Review
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Karyopherin-mediated nucleocytoplasmic transport.Nature reviews. Molecular cell biology · 2022
    Review
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors at 3 institutions in 2 countries.

Valentin MittererInstitut für Molekulare Biowissenschaften, Universität Graz, Humboldtstrasse 50, 8010 Graz, Austria.
Nadine GantenbeinInstitut für Molekulare Biowissenschaften, Universität Graz, Humboldtstrasse 50, 8010 Graz, Austria.
Ruth Birner-GruenbergerInstitute of Pathology, Research Unit Functional Proteomics and Metabolic Pathways, Medical University of Graz, Stiftingtalstrasse 24, 8010 Graz, Austria.
Guillaume MuratUnit of Biochemistry, Department of Biology, University of Fribourg, Chemin du Musée 10, CH-1700 Fribourg, Switzerland.
Helmut BerglerInstitut für Molekulare Biowissenschaften, Universität Graz, Humboldtstrasse 50, 8010 Graz, Austria.
Dieter KresslerUnit of Biochemistry, Department of Biology, University of Fribourg, Chemin du Musée 10, CH-1700 Fribourg, Switzerland.
Brigitte PertschyInstitut für Molekulare Biowissenschaften, Universität Graz, Humboldtstrasse 50, 8010 Graz, Austria.
University of Graz · ATUniversity of Fribourg · CHBioTechMed-Graz · AT

Funding

Austrian Science Fund FWF KLI 425Austrian Science Fund FWF P 26136Austrian Science Fund FWF P 28874
6 · The paper itself

Abstract

After their cytoplasmic synthesis, ribosomal proteins need to be transported into the nucleus, where they assemble with ribosomal RNA into pre-ribosomal particles. Due to their physicochemical properties, they need protection from aggregation on this path. Newly synthesized ribosomal protein Rps3 forms a dimer that is associated with one molecule of its specific chaperone Yar1. Here we report that redundant pathways contribute to the nuclear import of Rps3, with the classical importin α/β pathway (Kap60/Kap95 in yeast) constituting a main import route. The Kap60/Kap95 heterodimer mediates efficient nuclear import of Rps3 by recognition of an N-terminal monopartite nuclear localization signal (NLS). This Rps3-NLS is located directly adjacent to the Yar1-binding site and, upon binding of Kap60 to Rps3, Yar1 is displaced from the ribosomal protein in vitro. While Yar1 does not directly interact with Kap60 in vitro, affinity purifications of Yar1 and Rps3, however, revealed that Kap60 is present in the Rps3/Yar1 complex in vivo. Indeed we could reconstitute such a protein complex containing Rps3 and both Yar1 and Kap60 in vitro. Our data suggest that binding of Yar1 to one N-domain and binding of Kap60 to the second N-domain of dimerized Rps3 orchestrates import and protection of the ribosomal protein.

Indexed as

Active Transport, Cell Nucleusalpha Karyopherinsbeta KaryopherinsCell NucleusCytoplasmMicroscopy, FluorescenceMolecular ChaperonesNuclear Localization SignalsProtein BindingProtein DomainsRibosomal ProteinsRibosomesSaccharomyces cerevisiaeSaccharomyces cerevisiae Proteinsalpha Karyopherinsbeta KaryopherinsKAP95 protein, S cerevisiaeMolecular ChaperonesNuclear Localization SignalsRibosomal Proteinsribosomal protein S3RPS3 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsYAR1 protein, S cerevisiae

Identifiers

PMID27819319
PMCPMC5098186
OpenAlexW2549250343

What OpenQuestion holds

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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.