Evidence map›Paper›PMID 18647749›Full record

ArticleThe Journal of biological chemistry2008

G9a-mediated lysine methylation alters the function of CCAAT/enhancer-binding protein-beta.

Ole Pless, Elisabeth Kowenz-Leutz, Maria Knoblich, Jörn Lausen, Michael Beyermann, Martin J Walsh, Achim Leutz

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 71 papers.

0numbers the graph read from it
0cells of the map it votes in
71citing papers in PubMed
2.8field-weighted citation impact, top 10% 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

71 citing papers in PubMed, 106 citations in OpenAlex.

  1. Exosome Proteomics of SOD1Annals of clinical and translational neurology · 2026
    Article
  2. Review
  3. Review
  4. Lysine and arginine methylation of transcription factors.Cellular and molecular life sciences : CMLS · 2024
    Review
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Cell-specific expression of theFrontiers in molecular biosciences · 2023
    Article
  14. Article
  15. Review
  16. Review
  17. Targets of histone H3 lysine 9 methyltransferases.Frontiers in cell and developmental biology · 2022
    Review
  18. Article
  19. Article
  20. Review

11 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 at 4 institutions in 2 countries.

Ole PlessMax Delbrück Center for Molecular Medicine, Humboldt University of Berlin, Berlin, Germany.
Elisabeth Kowenz-Leutz
Maria Knoblich
Jörn Lausen
Michael Beyermann
Martin J Walsh
Achim Leutz
Max Delbrück Center · DEGeorg Speyer Haus · DEIcahn School of Medicine at Mount Sinai · USLeibniz Institute for Neurobiology · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The functional capacity of the transcriptional regulatory CCAAT/enhancer-binding protein-beta (C/EBPbeta) is governed by protein interactions and post-translational protein modifications. In a proteome-wide interaction screen, the histone-lysine N-methyltransferase, H3 lysine 9-specific 3 (G9a), was found to directly interact with the C/EBPbeta transactivation domain (TAD). Binding between G9a and C/EBPbeta was confirmed by glutathione S-transferase pulldown and co-immunoprecipitation. Metabolic labeling showed that C/EBPbeta is post-translationally modified by methylation in vivo. A conserved lysine residue in the C/EBPbeta TAD served as a substrate for G9a-mediated methylation. G9a, but not a methyltransferase-defective G9a mutant, abrogated the transactivation potential of wild type C/EBPbeta. A C/EBPbeta TAD mutant that contained a lysine-to-alanine exchange was resistant to G9a-mediated inhibition. Moreover, the same mutation conferred super-activation of a chromatin-embedded, endogenous C/EBPbeta target gene. Our data identify C/EBPbeta as a direct substrate of G9a-mediated post-translational modification that alters the functional properties of C/EBPbeta during gene regulation.

Indexed as

CCAAT-Enhancer-Binding Protein-betaHeLa CellsHistocompatibility AntigensHistone-Lysine N-MethyltransferaseHumansMutationProtein Processing, Post-TranslationalProtein Structure, TertiaryProteomeTranscriptional ActivationCCAAT-Enhancer-Binding Protein-betaEHMT2 protein, humanHistocompatibility AntigensHistone-Lysine N-MethyltransferaseProteome

Identifiers

PMID18647749
PMCPMC3258912
OpenAlexW2014970076

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.