Evidence map›Paper›PMID 11114158›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2000

Acetylation of adenovirus E1A regulates binding of the transcriptional corepressor CtBP.

Q Zhang, H Yao, N Vo, R H Goodman

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.

0numbers the graph read from it
0cells of the map it votes in
58citing papers in PubMed
4.5field-weighted citation impact, top 5% 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

58 citing papers in PubMed, 129 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Role of Ribeye PXDLS/T-binding cleft in normal synaptic ribbon function.bioRxiv : the preprint server for biology · 2023
    Article
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  12. Histone and Non-Histone Targets of Dietary Deacetylase Inhibitors.Current topics in medicinal chemistry · 2016
    Review
  13. Article
  14. Article
  15. Article
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  18. Review
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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

4 authors at 2 institutions in 1 country.

Q ZhangVollum Institute, Oregon Health Sciences University, Portland, OR 97201, USA.
H Yao
N Vo
R H Goodman
Vollum Institute · USOregon Health & Science University · US

Funding

UV regulation of anti-apoptotic co-repressor CtBPR01CA115468 · NCI · UNIVERSITY OF COLORADO DENVER · PI ZHANG, QINGHONG · 2007 to 2011
$1.4M
NCI NIH HHS R01 CA115468
6 · The paper itself

Abstract

Adenovirus E1A mediates its effects on cellular transformation and transcription by interacting with critical cellular proteins involved in cell growth and differentiation. The amino terminus of E1A binds to CBP/p300 and associated histone acetyltransferases such as P/CAF. The carboxyl terminus binds to the carboxyl-terminal binding protein (CtBP), which associates with histone deacetylases. We show that 12S E1A can be acetylated by p300 and P/CAF and map one of the acetylation sites to Lys-239. This Lys residue is adjacent to the consensus CtBP binding motif, PXDLS. Mutation of Lys-239 to Gln or Ala blocks CtBP binding in vitro and disrupts the E1A-CtBP interaction in vivo. Peptide competition assays demonstrated that the interaction of E1A with CtBP is also blocked by Lys-239 acetylation. Supporting a functional role for Lys-239 in CtBP binding, mutation of this residue to Ala decreases the ability of E1A to block cAMP-regulated enhancer (CRE)-binding protein (CREB)-stimulated gene expression. Finally, we demonstrate that Lys-239 is acetylated in cells by using an antibody directed against an acetyl-Lys-239 E1A peptide. CtBP interacts with a wide variety of other transcriptional repressors through the PXDLS motif, and, in many instances, this motif is followed by a Lys residue. We suggest that acetylation of this residue by histone acetyltransferases, and the consequent disruption of repressor complexes, might be a general mechanism for gene activation.

Indexed as

AcetylationAcetyltransferasesAdenovirus E1A ProteinsAlcohol OxidoreductasesAnimalsBinding SitesCell Cycle ProteinsChlorocebus aethiopsCOS CellsCREB-Binding ProteinDNA-Binding ProteinsGene Expression RegulationGenes, ReporterHistone AcetyltransferasesHumansLuciferasesAcetyltransferasesAdenovirus E1A ProteinsAlcohol OxidoreductasesCell Cycle ProteinsCREB-Binding ProteinCREBBP protein, humanC-terminal binding proteinDNA-Binding ProteinsHistone AcetyltransferasesLuciferasesLysineNuclear Proteinsp300-CBP-Associated Factorp300-CBP Transcription FactorsPhosphoproteinsRepressor ProteinsTrans-ActivatorsTranscription Factors

Identifiers

PMID11114158
PMCPMC18917
OpenAlexW2096005665

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.