Evidence map›Paper›PMID 16371476›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2006

PDSM, a motif for phosphorylation-dependent SUMO modification.

Ville Hietakangas, Julius Anckar, Henri A Blomster, Mitsuaki Fujimoto, Jorma J Palvimo, Akira Nakai, Lea Sistonen

Abstract readComparative Study
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 260 papers.

0numbers the graph read from it
0cells of the map it votes in
260citing 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

260 citing papers in PubMed.

  1. Review
  2. Review
  3. A Landscape Analysis of Human SUMOylation.Molecular & cellular proteomics : MCP · 2026
    Article
  4. Review
  5. Article
  6. Review
  7. Review
  8. Article
  9. Review
  10. Article
  11. Article
  12. Review
  13. HSF1 Activation Mechanisms, Disease Roles, and Small Molecule Therapeutics.International journal of biological sciences · 2025
    Review
  14. Multifaceted roles of SUMO in DNA metabolism.Nucleus (Austin, Tex.) · 2024
    Review
  15. Article
  16. Posttranslational Modifications ofPharmacological reviews · 2024
    Review
  17. Article
  18. Review
  19. Article
  20. Article

200 more citing papers are in PubMed but not listed here.

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.

Ville HietakangasTurku Centre for Biotechnology, University of Turku and Abo Akademi University, FI-20521, Turku, Finland.
Julius Anckar
Henri A Blomster
Mitsuaki Fujimoto
Jorma J Palvimo
Akira Nakai
Lea Sistonen

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

SUMO (small ubiquitin-like modifier) modification regulates many cellular processes, including transcription. Although sumoylation often occurs on specific lysines within the consensus tetrapeptide PsiKxE, other modifications, such as phosphorylation, may regulate the sumoylation of a substrate. We have discovered PDSM (phosphorylation-dependent sumoylation motif), composed of a SUMO consensus site and an adjacent proline-directed phosphorylation site (PsiKxExxSP). The highly conserved motif regulates phosphorylation-dependent sumoylation of multiple substrates, such as heat-shock factors (HSFs), GATA-1, and myocyte enhancer factor 2. In fact, the majority of the PDSM-containing proteins are transcriptional regulators. Within the HSF family, PDSM is conserved between two functionally distinct members, HSF1 and HSF4b, whose transactivation capacities are repressed through the phosphorylation-dependent sumoylation. As the first recurrent sumoylation determinant beyond the consensus tetrapeptide, the PDSM provides a valuable tool in predicting new SUMO substrates.

Indexed as

Amino Acid MotifsBlotting, WesternConsensus SequenceElectrophoretic Mobility Shift AssayHeat-Shock ProteinsImmunoprecipitationLuciferasesPhosphorylationRegulatory Elements, TranscriptionalReverse Transcriptase Polymerase Chain ReactionSmall Ubiquitin-Related Modifier ProteinsHeat-Shock ProteinsLuciferasesSmall Ubiquitin-Related Modifier Proteins

Identifiers

PMID16371476
PMCPMC1324973

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.