Evidence map›Paper›PMID 25144938›Full record

ArticleeLife2014

A RanGTP-independent mechanism allows ribosomal protein nuclear import for ribosome assembly.

Sabina Schütz, Ute Fischer, Martin Altvater, Purnima Nerurkar, Cohue Peña, Michaela Gerber, Yiming Chang, Stefanie Caesar, Olga T Schubert, Gabriel Schlenstedt and 1 more

Abstract read
In one paragraph

Article in eLife, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.

0numbers the graph read from it
0cells of the map it votes in
58citing 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

58 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Ribosome Assembly and Repair.Annual review of cell and developmental biology · 2024
    Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. The homeostatic regulation of ribosome biogenesis.Seminars in cell & developmental biology · 2023
    Review
  17. Karyopherin-mediated nucleocytoplasmic transport.Nature reviews. Molecular cell biology · 2022
    Review
  18. Article
  19. Article
  20. 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

11 authors.

Sabina SchützInstitute of Biochemistry, Department of Biology, ETH Zurich, Zurich, Switzerland Molecular Life Science Graduate School, University of Zurich, Zurich, Switzerland.
Ute FischerInstitute of Biochemistry, Department of Biology, ETH Zurich, Zurich, Switzerland.
Martin AltvaterInstitute of Biochemistry, Department of Biology, ETH Zurich, Zurich, Switzerland Molecular Life Science Graduate School, University of Zurich, Zurich, Switzerland.
Purnima NerurkarInstitute of Biochemistry, Department of Biology, ETH Zurich, Zurich, Switzerland Molecular Life Science Graduate School, University of Zurich, Zurich, Switzerland.
Cohue PeñaInstitute of Biochemistry, Department of Biology, ETH Zurich, Zurich, Switzerland.
Michaela GerberInstitute of Biochemistry, Department of Biology, ETH Zurich, Zurich, Switzerland.
Yiming ChangInstitute of Biochemistry, Department of Biology, ETH Zurich, Zurich, Switzerland.
Stefanie CaesarInstitute of Medical Biochemistry and Molecular Biology, Universität des Saarlandes, Homburg, Germany.
Olga T SchubertInstitute of Molecular Systems Biology, Department of Biology, ETH Zurich, Zurich, Switzerland Systems Biology Graduate School, Zurich, Zurich, Switzerland.
Gabriel SchlenstedtInstitute of Medical Biochemistry and Molecular Biology, Universität des Saarlandes, Homburg, Germany.
Vikram G PanseInstitute of Biochemistry, Department of Biology, ETH Zurich, Zurich, Switzerland vikram.panse@bc.biol.ethz.ch.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Within a single generation time a growing yeast cell imports ∼14 million ribosomal proteins (r-proteins) into the nucleus for ribosome production. After import, it is unclear how these intrinsically unstable and aggregation-prone proteins are targeted to the ribosome assembly site in the nucleolus. Here, we report the discovery of a conserved nuclear carrier Tsr2 that coordinates transfer of the r-protein eS26 to the earliest assembling pre-ribosome, the 90S. In vitro studies revealed that Tsr2 efficiently dissociates importin:eS26 complexes via an atypical RanGTP-independent mechanism that terminates the import process. Subsequently, Tsr2 binds the released eS26, shields it from proteolysis, and ensures its safe delivery to the 90S pre-ribosome. We anticipate similar carriers-termed here escortins-to securely connect the nuclear import machinery with pathways that deposit r-proteins onto developing pre-ribosomal particles.

Indexed as

Active Transport, Cell NucleusAmino Acid Sequencebeta KaryopherinsCarrier ProteinsCell NucleusEscherichia coliGTPase-Activating ProteinsKaryopherinsMolecular Sequence DataProtein BindingProtein StabilityProteolysisRecombinant ProteinsRibosomal ProteinsRibosomesRNA, Ribosomal, 18Sbeta KaryopherinsCarrier ProteinsGTPase-Activating ProteinsKAP104 protein, S cerevisiaeKap123 protein, S cerevisiaeKaryopherinsRecombinant ProteinsRibosomal ProteinsRNA, Ribosomal, 18SSaccharomyces cerevisiae ProteinsDiamond-Blackfan anemia (DBA)eS26nuclear importribosome biogenesisrRNA processingTsr2

Identifiers

PMID25144938
PMCPMC4161973

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.