Evidence map›Paper›PMID 19596686›Full record

ArticleMolecular & cellular proteomics : MCP2009

Proteomics analysis of nucleolar SUMO-1 target proteins upon proteasome inhibition.

Vittoria Matafora, Alfonsina D'Amato, Silvia Mori, Francesco Blasi, Angela Bachi

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.

0numbers the graph read from it
0cells of the map it votes in
57citing papers in PubMed
3.2field-weighted citation impact, top 8% 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

57 citing papers in PubMed, 94 citations in OpenAlex.

  1. Ribosome-associated proteins: unwRAPping ribosome heterogeneity in the twenty-first century.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2025
    Review
  2. Review
  3. Article
  4. Article
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  7. Regulation of SUMOylation on RNA metabolism in cancers.Frontiers in molecular biosciences · 2023
    Review
  8. Article
  9. Article
  10. Histone sumoylation and chromatin dynamics.Nucleic acids research · 2021
    Review
  11. Article
  12. Article
  13. Article
  14. An interaction between PRRT2 and NaCell death & disease · 2021
    Article
  15. Review
  16. Article
  17. Article
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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

5 authors at 2 institutions in 1 country.

Vittoria MataforaDivision of Genomics and Cell Biology, San Raffaele Scientific Institute, Milan, Italy.
Alfonsina D'Amato
Silvia Mori
Francesco Blasi
Angela Bachi
FIRC Institute of Molecular Oncology · ITVita-Salute San Raffaele University · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Many cellular processes are regulated by the coordination of several post-translational modifications that allow a very fine modulation of substrates. Recently it has been reported that there is a relationship between sumoylation and ubiquitination. Here we propose that the nucleolus is the key organelle in which SUMO-1 conjugates accumulate in response to proteasome inhibition. We demonstrated that, upon proteasome inhibition, the SUMO-1 nuclear dot localization is redirected to nucleolar structures. To better understand this process we investigated, by quantitative proteomics, the effect of proteasome activity on endogenous nucleolar SUMO-1 targets. 193 potential SUMO-1 substrates were identified, and interestingly in several purified SUMO-1 conjugates ubiquitin chains were found to be present, confirming the coordination of these two modifications. 23 SUMO-1 targets were confirmed by an in vitro sumoylation reaction performed on nuclear substrates. They belong to protein families such as small nuclear ribonucleoproteins, heterogeneous nuclear ribonucleoproteins, ribosomal proteins, histones, RNA-binding proteins, and transcription factor regulators. Among these, histone H1, histone H3, and p160 Myb-binding protein 1A were further characterized as novel SUMO-1 substrates. The analysis of the nature of the SUMO-1 targets identified in this study strongly indicates that sumoylation, acting in coordination with the ubiquitin-proteasome system, regulates the maintenance of nucleolar integrity.

Indexed as

Proteasome InhibitorsProtein Processing, Post-TranslationalAnimalsCell NucleolusCysteine Proteinase InhibitorsHeLa CellsHumansIsotope LabelingLeupeptinsMolecular Sequence DataProteomicsSUMO-1 Proteinbenzyloxycarbonylleucyl-leucyl-leucine aldehydeCysteine Proteinase InhibitorsLeupeptinsProteasome InhibitorsSUMO-1 Protein

Identifiers

PMID19596686
PMCPMC2758753
OpenAlexW2119456552

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.