Evidence map›Paper›PMID 11486036›Full record

ArticleMolecular and cellular biology2001

Regulation of transcription factor YY1 by acetylation and deacetylation.

Y L Yao, W M Yang, E Seto

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 213 papers.

0numbers the graph read from it
0cells of the map it votes in
213citing papers in PubMed
8.0field-weighted citation impact, top 2% 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

213 citing papers in PubMed, 438 citations in OpenAlex.

  1. Article
  2. Review
  3. mNature metabolism · 2026
    Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. The YYR (YY1- RKIP) Regulatory Axis in the pathogenesis of Cancer and Immune Evasion.Journal of experimental & clinical cancer research : CR · 2025
    Review
  14. Review
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. Article

153 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

3 authors at 1 institution in 1 country.

Y L YaoDepartment of Medical Microbiology and Immunology, Interdisciplinary Oncology Program, H. Lee Moffitt Cancer Center and Research Institute, College of Medicine, University of South Florida, Tampa, FL 33612, USA.
W M Yang
E Seto
University of South Florida · US

Funding

FUNCTIONAL ANALYSIS OF MAMMALIAN HISTONE DEACETYLASESR01GM058486 · NIGMS · UNIVERSITY OF SOUTH FLORIDA · PI SETO, EDWARD · 1999 to 2006
$2.3M
NIGMS NIH HHS GM58486NIGMS NIH HHS R01 GM058486
6 · The paper itself

Abstract

YY1 is a sequence-specific DNA-binding transcription factor that has many important biological roles. It activates or represses many genes during cell growth and differentiation and is also required for the normal development of mammalian embryos. Previous studies have established that YY1 interacts with histone acetyltransferases p300 and CREB-binding protein (CBP) and histone deacetylase 1 (HDAC1), HDAC2, and HDAC3. Here, we present evidence that the activity of YY1 is regulated through acetylation by p300 and PCAF and through deacetylation by HDACs. YY1 was acetylated in two regions: both p300 and PCAF acetylated the central glycine-lysine-rich domain of residues 170 to 200, and PCAF also acetylated YY1 at the C-terminal DNA-binding zinc finger domain. Acetylation of the central region was required for the full transcriptional repressor activity of YY1 and targeted YY1 for active deacetylation by HDACs. However, the C-terminal region of YY1 could not be deacetylated. Rather, the acetylated C-terminal region interacted with HDACs, which resulted in stable HDAC activity associated with the YY1 protein. Finally, acetylation of the C-terminal zinc finger domain decreased the DNA-binding activity of YY1. Our findings suggest that in the natural context, YY1 activity is regulated through intricate mechanisms involving negative feedback loops, histone deacetylation, and recognition of the cognate DNA sequence affected by acetylation and deacetylation of the YY1 protein.

Indexed as

AcetylationSaccharomyces cerevisiae ProteinsAcetyltransferasesAmino Acid SequenceArginineBinding SitesDNADNA-Binding ProteinsErythroid-Specific DNA-Binding FactorsHeLa CellsHistone AcetyltransferasesHistone Deacetylase 1Histone Deacetylase 2Histone Deacetylase 3Histone DeacetylasesHumansAcetyltransferasesArginineDNADNA-Binding ProteinsErythroid-Specific DNA-Binding FactorsHDAC1 protein, humanHistone AcetyltransferasesHistone Deacetylase 1Histone Deacetylase 2Histone Deacetylase 3Histone DeacetylasesLysineNuclear ProteinsRecombinant Fusion ProteinsRepressor ProteinsSaccharomyces cerevisiae ProteinsTrans-ActivatorsTranscription FactorsYY1 protein, humanYY1 Transcription Factor

Identifiers

PMID11486036
PMCPMC87316
OpenAlexW2164380111

What OpenQuestion holds

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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.