Evidence map›Paper›PMID 28951443›Full record

ArticleMolecular & cellular proteomics : MCP2017

Converging Small Ubiquitin-like Modifier (SUMO) and Ubiquitin Signaling: Improved Methodology Identifies Co-modified Target Proteins.

Sabine A G Cuijpers, Edwin Willemstein, Alfred C O Vertegaal

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
1.5field-weighted citation impact, top 18% 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

23 citing papers in PubMed, 28 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Review
  5. Review
  6. Article
  7. Solo or in Concert: SUMOylation in Pathogenic Fungi.The plant pathology journal · 2025
    Review
  8. Article
  9. Article
  10. SUMO/deSUMOylation of the BRI1 brassinosteroid receptor modulates plant growth responses to temperature.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Review
  16. Decoding the PTM-switchboard of Notch.Biochimica et biophysica acta. Molecular cell research · 2019
    Review
  17. Article
  18. Review
  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

3 authors at 1 institution in 1 country.

Sabine A G CuijpersFrom the ‡Department of Molecular Cell Biology, Leiden University Medical Center, 2300 RC Leiden, the Netherlands.
Edwin WillemsteinFrom the ‡Department of Molecular Cell Biology, Leiden University Medical Center, 2300 RC Leiden, the Netherlands.
Alfred C O VertegaalFrom the ‡Department of Molecular Cell Biology, Leiden University Medical Center, 2300 RC Leiden, the Netherlands vertegaal@lumc.nl.
Leiden University Medical Center · NL

Funding

European Research Council 310913
6 · The paper itself

Abstract

Post-translational protein modifications (PTMs) including small chemical groups and small proteins, belonging to the ubiquitin family, are essential for virtually all cellular processes. In addition to modification by a single PTM, proteins can be modified by a combination of different modifiers, which are able to influence each other. Because little is known about crosstalk among different ubiquitin family members, we developed an improved method enabling identification of co-modified proteins on a system-wide level using mass spectrometry. We focused on the role of crosstalk between SUMO and ubiquitin during proteasomal degradation. Using two complementary approaches, we identified 498 proteins to be significantly co-modified by SUMO and ubiquitin upon MG132 treatment. These targets included many enzymatic components of PTM machinery, involved in SUMOylation and ubiquitylation, but also phosphorylation, methylation and acetylation, revealing a highly complex interconnected network of crosstalk among different PTMs. In addition, various other biological processes were found to be significantly enriched within the group of co-modified proteins, including transcription, DNA repair and the cell cycle. Interestingly, the latter group mostly consisted of proteins involved in mitosis, including a subset of chromosome segregation regulators. We hypothesize that group modification by SUMO-targeted ubiquitin ligases regulates the stability of the identified subset of mitotic proteins, which ensures proper chromosome segregation. The mitotic regulators KIF23 and MIS18BP1 were verified to be co-modified by SUMO and ubiquitin on inhibition of the proteasome and subsequently identified as novel RNF4 targets. Both modifications on MIS18BP1 were observed to increase simultaneously during late mitosis, whereas the total protein level decreased immediately afterward. These results confirm the regulation of MIS18BP1 via SUMO-ubiquitin crosstalk during mitosis. Combined, our work highlights extensive crosstalk between SUMO and ubiquitin, providing a resource for further unraveling of SUMO-ubiquitin crosstalk.

Indexed as

Cell LineChromosomal Proteins, Non-HistoneGene Regulatory NetworksHEK293 CellsHumansLeupeptinsMicrotubule-Associated ProteinsMitosisNuclear ProteinsProtein Interaction MapsProteomicsSmall Ubiquitin-Related Modifier ProteinsSumoylationTranscription FactorsUbiquitinationUbiquitinsbenzyloxycarbonylleucyl-leucyl-leucine aldehydeChromosomal Proteins, Non-HistoneKIF23 protein, humanLeupeptinsMicrotubule-Associated ProteinsMIS18BP1 protein, humanNuclear ProteinsRNF4 protein, humanSmall Ubiquitin-Related Modifier ProteinsTranscription FactorsUbiquitins

Identifiers

PMID28951443
PMCPMC5724187
OpenAlexW2757408688

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

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.