Evidence map›Paper›PMID 17332356›Full record

ArticleCancer research2007

Histone deacetylase inhibitors synergize p300 autoacetylation that regulates its transactivation activity and complex formation.

Daniel P Stiehl, Donna M Fath, Dongming Liang, Yubao Jiang, Nianli Sang

Open access · bronzeAbstract read
In one paragraph

Article in Cancer research, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

27 citing papers in PubMed, 66 citations in OpenAlex.

  1. Article
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  7. Sirt7 inhibits Sirt1-mediated activation of Suv39h1.Cell cycle (Georgetown, Tex.) · 2018
    Article
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  18. Design of small molecule epigenetic modulators.Bioorganic & medicinal chemistry letters · 2014
    Review
  19. The Roles of SIRT1 in Cancer.Genes & cancer · 2013
    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

5 authors at 2 institutions in 1 country.

Daniel P Stiehl *Cardeza Foundation for Hematologic Research, Department of Medicine, Thomas Jefferson University, Philadelphia, Pennsylvania.
Donna M Fath *Cardeza Foundation for Hematologic Research, Department of Medicine, Thomas Jefferson University, Philadelphia, Pennsylvania.
Dongming LiangCardeza Foundation for Hematologic Research, Department of Medicine, Thomas Jefferson University, Philadelphia, Pennsylvania.
Yubao JiangCardeza Foundation for Hematologic Research, Department of Medicine, Thomas Jefferson University, Philadelphia, Pennsylvania.
Nianli SangCardeza Foundation for Hematologic Research, Department of Medicine, Thomas Jefferson University, Philadelphia, Pennsylvania.
Sidney Kimmel Cancer Center · USThomas Jefferson University · US

Funding

Transactivating of Activity of HIF-1 in tumorigenesisK01CA098809 · NCI · THOMAS JEFFERSON UNIVERSITY · PI SANG, NIANLI · 2003 to 2007
$714k
NCI NIH HHS CA 098809NCI NIH HHS K01 CA098809
6 · The paper itself

Abstract

p300/cyclic AMP-responsive element binding protein-binding protein (CBP) are general coactivators for multiple transcription factors involved in various cellular processes. Several highly conserved domains of p300/CBP serve as interacting sites for transcription factors and regulatory proteins. Particularly, the intrinsic histone acetyltransferase (HAT) activity and transactivation domains (TAD) play essential roles for their coactivating function. Autoacetylation of p300/CBP is commonly observed in cell-free HAT assays and has been implicated in the regulation of their HAT activity. Here, we show that six lysine-rich regions in several highly conserved functional domains of p300 are targeted by p300HAT for acetylation in cell-free systems. We show that p300 is susceptible to acetylation in cultured tumor cells and that its acetylation status is affected by histone deacetylase inhibitor trichostatin A. We further show that either treatment with deacetylase inhibitors or coexpression of Gal4-p300HAT, which alone has no transactivation activity, stimulates the activity of the COOH-terminal TAD of p300 (p300C-TAD). We have defined the minimal p300C-TAD and show that it is sufficient to respond to deacetylase inhibitors and is a substrate for p300HAT. Finally, we show that acetylated p300 possesses enhanced ability to interact with p53. Taken together, our data suggest that acetylation regulates p300C-TAD and that acetylation of p300/CBP may contribute to the dynamic regulation of their complex formation with various interacting partners.

Indexed as

Histone Deacetylase InhibitorsAcetylationAmino Acid SequenceCatalytic DomainCell Cycle ProteinsCells, CulturedHeLa CellsHistone AcetyltransferasesHumansHydroxamic AcidsMolecular Sequence Datap300-CBP-Associated Factorp300-CBP Transcription FactorsProtein BindingProtein Structure, TertiarySequence Homology, Amino AcidCell Cycle ProteinsHistone AcetyltransferasesHistone Deacetylase InhibitorsHydroxamic Acidsp300-CBP-Associated Factorp300-CBP Transcription FactorsTranscription Factorstrichostatin A

Identifiers

PMID17332356
PMCPMC4526273
OpenAlexW2096015427

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.