Evidence map›Paper›PMID 17636029›Full record

ArticleMolecular and cellular biology2007

Tip60 histone acetyltransferase acts as a negative regulator of Notch1 signaling by means of acetylation.

Mi-Yeon Kim, Eun-Jung Ann, Jin-Young Kim, Jung-Soon Mo, Ji-Hye Park, Sun-Yee Kim, Mi-Sun Seo, Hee-Sae Park

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

24 citing papers in PubMed, 49 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
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  7. Article
  8. Interaction of the epigenetic integrator UHRF1 with the MYST domain of TIP60 inside the cell.Journal of experimental & clinical cancer research : CR · 2017
    Article
  9. Article
  10. Acetylation promotes TyrRS nuclear translocation to prevent oxidative damage.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Notch1 modulates oxidative stress induced cell death through suppression of apoptosis signal-regulating kinase 1.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. MYST-family histone acetyltransferases: beyond chromatin.Cellular and molecular life sciences : CMLS · 2011
    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

8 authors at 1 institution in 1 country.

Mi-Yeon KimHormonre Research Center, School of Biological Sciences and Technology, Chonnam National University, Yongbong-dong, Buk-ku, Gwangju 500-757, South Korea.
Eun-Jung Ann
Jin-Young Kim
Jung-Soon Mo
Ji-Hye Park
Sun-Yee Kim
Mi-Sun Seo
Hee-Sae Park
Chonnam National University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Notch signaling pathway appears to perform an important function in a wide variety of organisms and cell types. In our present study, we provide evidence that UV irradiation-induced Tip60 proteins reduced Notch1 activity to a marked degree. Accumulated UV irradiation-induced Tip60 suppresses Notch1 transcriptional activity via the dissociation of the Notch1-IC-CSL complex. The binding between endogenous Tip60 and Notch1-IC in UV radiation-exposed cells was verified in this study by coimmunoprecipitation. Interestingly, the physical interaction of Tip60 with Notch1-IC occurs to a more profound degree in the presence of CSL but does not exist in a trimeric complex. Using Notch1-IC and Tip60 deletion mutants, we also determined that the N terminus, which harbors the RAM domain and seven ankyrin repeats of Notch1-IC, interacts with the zinc finger and acetyl coenzyme A domains of Tip60. Furthermore, here we report that Notch1-IC is a direct target of the acetyltransferase activity of Tip60. Collectively, our data suggest that Tip60 is an inhibitor of the Notch1 signaling pathway and that Tip60-dependent acetylation of Notch1-IC may be relevant to the mechanism by which Tip60 suppresses Notch1 signaling.

Indexed as

Signal TransductionAcetylationAnimalsCell LineEscherichia coliGene DeletionGenes, ReporterGlutathione TransferaseHistone AcetyltransferasesHumansKidneyLuciferasesLysine Acetyltransferase 5MiceModels, BiologicalNIH 3T3 CellsGlutathione TransferaseHistone AcetyltransferasesKAT5 protein, humanKat5 protein, mouseLuciferasesLysine Acetyltransferase 5NOTCH1 protein, humanNotch1 protein, mouseReceptor, Notch1Recombinant ProteinsTrans-Activators

Identifiers

PMID17636029
PMCPMC2099611
OpenAlexW2131679975

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.