Evidence map›Paper›PMID 23043228›Full record

ArticleBMC biochemistry2012

Structure-function analysis indicates that sumoylation modulates DNA-binding activity of STAT1.

Juha Grönholm, Sari Vanhatupa, Daniela Ungureanu, Jouni Väliaho, Tuomo Laitinen, Jarkko Valjakka, Olli Silvennoinen

Open access · hybridAbstract read
In one paragraph

Article in BMC biochemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
0.8field-weighted citation impact, top 27% 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

16 citing papers in PubMed, 31 citations in OpenAlex.

  1. Article
  2. An atlas of protein phosphorylation dynamics during interferon signaling.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  3. Article
  4. Article
  5. Article
  6. SUMO and Cytoplasmic RNA Viruses: From Enemies to Best Friends.Advances in experimental medicine and biology · 2020
    Review
  7. Article
  8. Article
  9. Responses to Cytokines and Interferons that Depend upon JAKs and STATs.Cold Spring Harbor perspectives in biology · 2018
    Review
  10. Article
  11. Review
  12. Article
  13. Review
  14. Article
  15. Article
  16. Review
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.

Juha GrönholmInstitute of Biomedical Technology, University of Tampere, Biokatu 8, Tampere, FIN-33014, Finland.
Sari Vanhatupa
Daniela Ungureanu
Jouni Väliaho
Tuomo Laitinen
Jarkko Valjakka
Olli Silvennoinen
Tampere University · FIUniversity of Eastern Finland · FI

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundSTAT1 is an essential transcription factor for interferon-γ-mediated gene responses. A distinct sumoylation consensus site (ψKxE) 702IKTE705 is localized in the C-terminal region of STAT1, where Lys703 is a target for PIAS-induced SUMO modification. Several studies indicate that sumoylation has an inhibitory role on STAT1-mediated gene expression but the molecular mechanisms are not fully understood.

resultsHere, we have performed a structural and functional analysis of sumoylation in STAT1. We show that deconjugation of SUMO by SENP1 enhances the transcriptional activity of STAT1, confirming a negative regulatory effect of sumoylation on STAT1 activity. Inspection of molecular model indicated that consensus site is well exposed to SUMO-conjugation in STAT1 homodimer and that the conjugated SUMO moiety is directed towards DNA, thus able to form a sterical hindrance affecting promoter binding of dimeric STAT1. In addition, oligoprecipitation experiments indicated that sumoylation deficient STAT1 E705Q mutant has higher DNA-binding activity on STAT1 responsive gene promoters than wild-type STAT1. Furthermore, sumoylation deficient STAT1 E705Q mutant displayed enhanced histone H4 acetylation on interferon-γ-responsive promoter compared to wild-type STAT1.

conclusionsOur results suggest that sumoylation participates in regulation of STAT1 responses by modulating DNA-binding properties of STAT1.

Indexed as

AcetylationAmino Acid SequenceAmino Acid SubstitutionAnimalsChlorocebus aethiopsChromatin ImmunoprecipitationCOS CellsCysteine EndopeptidasesDimerizationDNAEndopeptidasesHeLa CellsHistonesHumansPromoter Regions, GeneticProtein Structure, TertiaryCysteine EndopeptidasesDNAEndopeptidasesHistonesRecombinant ProteinsSENP1 protein, humanSTAT1 protein, humanSTAT1 Transcription Factor

Identifiers

PMID23043228
PMCPMC3532225
OpenAlexW2100802864

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LicenceCC BY
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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.