Evidence map›Paper›PMID 23242550›Full record

ArticleMolecular & cellular proteomics : MCP2013

Subcellular distribution and dynamics of active proteasome complexes unraveled by a workflow combining in vivo complex cross-linking and quantitative proteomics.

Bertrand Fabre, Thomas Lambour, Julien Delobel, François Amalric, Bernard Monsarrat, Odile Burlet-Schiltz, Marie-Pierre Bousquet-Dubouch

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
2.0field-weighted citation impact, top 13% 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

49 citing papers in PubMed, 100 citations in OpenAlex.

  1. Article
  2. Article
  3. MS-Based Proteomics Approach in Mapping Protein-Protein Interaction.Advances in experimental medicine and biology · 2026
    Review
  4. Review
  5. Review
  6. Article
  7. Article
  8. Article
  9. The Significant Role of PA28αβ in CD8International journal of molecular sciences · 2024
    Article
  10. Review
  11. Hats off to 20S proteasome substrate discovery.Molecular systems biology · 2024
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Review
  18. Review
  19. Proteasome complexes experience profound structural and functional rearrangements throughout mammalian spermatogenesis.Proceedings of the National Academy of Sciences of the United States of America · 2022
    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

7 authors at 2 institutions in 1 country.

Bertrand FabreCNRS/Institut de Pharmacologie et de Biologie Structurale, 205 route de Narbonne, Toulouse, France.
Thomas Lambour
Julien Delobel
François Amalric
Bernard Monsarrat
Odile Burlet-Schiltz
Marie-Pierre Bousquet-Dubouch
Institut de Pharmacologie et de Biologie Structurale · FRUniversité de Toulouse · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Through protein degradation, the proteasome plays fundamental roles in different cell compartments. Although the composition of the 20S catalytic core particle (CP) has been well documented, little is known about the composition and dynamics of the regulatory complexes that play a crucial role in its activity, or about how they associate with the CP in different cell compartments, different cell lines, and in response to external stimuli. Because of difficulties performing acceptable cell fractionation while maintaining complex integrity, it has been challenging to characterize proteasome complexes by proteomic approaches. Here, we report an integrated protocol, combining a cross-linking procedure on intact cells with cell fractionation, proteasome immuno-purification, and robust label-free quantitative proteomic analysis by mass spectrometry to determine the distribution and dynamics of cellular proteasome complexes in leukemic cells. Activity profiles of proteasomes were correlated fully with the composition of protein complexes and stoichiometry. Moreover, our results suggest that, at the subcellular level, proteasome function is regulated by dynamic interactions between the 20S CP and its regulatory proteins-which modulate proteasome activity, stability, localization, or substrate uptake-rather than by profound changes in 20S CP composition. Proteasome plasticity was observed both in the 20S CP and in its network of interactions following IFNγ stimulation. The fractionation protocol also revealed specific proteolytic activities and structural features of low-abundance microsomal proteasomes from U937 and KG1a cells. These could be linked to their important roles in the endoplasmic reticulum associated degradation pathway in leukemic cells.

Indexed as

Blotting, WesternCell Line, TumorCross-Linking ReagentsHumansInterferon-gammaIntracellular SpaceKineticsLeukemiaMass SpectrometryMicroscopy, ConfocalMicrosomesMultienzyme ComplexesProteasome Endopeptidase ComplexProtein BindingProtein SubunitsProteomicsCross-Linking ReagentsInterferon-gammaMultienzyme ComplexesProteasome Endopeptidase ComplexProtein Subunits

Identifiers

PMID23242550
PMCPMC3591661
OpenAlexW2136007082

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.