Evidence map›Paper›PMID 23982732›Full record

ArticleThe EMBO journal2013

Blm10 facilitates nuclear import of proteasome core particles.

Marion H Weberruss, Anca F Savulescu, Julia Jando, Thomas Bissinger, Amnon Harel, Michael H Glickman, Cordula Enenkel

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

39 citing papers in PubMed, 61 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Plasticity in the structure and assembly of proteasomes.The Journal of biological chemistry · 2026
    Review
  6. Article
  7. Proteasome dynamics in response to metabolic changes.Frontiers in cell and developmental biology · 2025
    Review
  8. Article
  9. Proteasome condensate formation is driven by multivalent interactions with shuttle factors and ubiquitin chains.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
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  11. Article
  12. Review
  13. Article
  14. Article
  15. Review
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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

7 authors at 5 institutions in 4 countries.

Marion H Weberruss1] Department of Biochemistry, University of Toronto, One King's College Circle, Toronto, Ontario, Canada [2] Institute of Biochemistry, University of Stuttgart, Stuttgart, Germany.
Anca F Savulescu
Julia Jando
Thomas Bissinger
Amnon Harel
Michael H Glickman
Cordula Enenkel
Technion – Israel Institute of Technology · ILUniversity of Stuttgart · DEBar-Ilan University · ILCanada Research Chairs · CAUniversity of Zurich · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Short-lived proteins are degraded by proteasome complexes, which contain a proteolytic core particle (CP) but differ in the number of regulatory particles (RPs) and activators. A recently described member of conserved proteasome activators is Blm10. Blm10 contains 32 HEAT-like modules and is structurally related to the nuclear import receptor importin/karyopherin β. In proliferating yeast, RP-CP assemblies are primarily nuclear and promote cell division. During quiescence, RP-CP assemblies dissociate and CP and RP are sequestered into motile cytosolic proteasome storage granuli (PSG). Here, we show that CP sequestration into PSG depends on Blm10, whereas RP sequestration into PSG is independent of Blm10. PSG rapidly clear upon the resumption of cell proliferation and proteasomes are relocated into the nucleus. Thereby, Blm10 facilitates nuclear import of CP. Blm10-bound CP serves as an import receptor-cargo complex, as Blm10 mediates the interaction with FG-rich nucleoporins and is dissociated from the CP by Ran-GTP. Thus, Blm10 represents the first CP-dedicated nuclear import receptor in yeast.

Indexed as

Active Transport, Cell NucleusAnimalsCell NucleusCell ProliferationCytoplasmic GranulesGreen Fluorescent ProteinsModels, BiologicalNuclear Pore Complex ProteinsOrganisms, Genetically ModifiedProteasome Endopeptidase ComplexReceptors, Cytoplasmic and NuclearSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsXenopusBlm10 protein, S cerevisiaeGreen Fluorescent ProteinsNuclear Pore Complex ProteinsNUP53 protein, S cerevisiaeProteasome Endopeptidase ComplexReceptors, Cytoplasmic and NuclearSaccharomyces cerevisiae Proteins

Identifiers

PMID23982732
PMCPMC3801435
OpenAlexW2073110368

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.