Evidence map›Paper›PMID 12840002›Full record

ArticleThe EMBO journal2003

A SANT motif in the SMRT corepressor interprets the histone code and promotes histone deacetylation.

Jiujiu Yu, Yun Li, Takahiro Ishizuka, Matthew G Guenther, Mitchell A Lazar

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 85 papers.

0numbers the graph read from it
0cells of the map it votes in
85citing papers in PubMed
6.9field-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

85 citing papers in PubMed, 180 citations in OpenAlex.

  1. Review
  2. Review
  3. Deep Sequencing Reveals Novel Mutations inInternational journal of molecular sciences · 2025
    Article
  4. Review
  5. Article
  6. Molecular Mechanism of Resistance toInternational journal of molecular sciences · 2024
    Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Review
  14. Loss of Long Noncoding RNACancer research · 2022
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

25 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

5 authors at 1 institution in 1 country.

Jiujiu YuDepartment of Medicine, University of Pennsylvania School of Medicine, Philadelphia, PA 19104-6149, USA.
Yun Li
Takahiro Ishizuka
Matthew G Guenther
Mitchell A Lazar
University of Pennsylvania · US

Funding

VIRAL VECTOR COREP30DK019525 · NIDDK · UNIVERSITY OF PENNSYLVANIA · PI MITCHELL A. LAZAR · 1986 to 2026
$48.3M
REV-ERB Nuclear Receptors in Circadian Rhythm and MetabolismR01DK045586 · NIDDK · UNIVERSITY OF PENNSYLVANIA · PI MITCHELL A. LAZAR · 1992 to 2026
$12.0M
THYROID HORMONE RECEPTORS-REGULATION AND FUNCTIONR37DK043806 · NIDDK · UNIVERSITY OF PENNSYLVANIA · PI LAZAR, MITCHELL A. · 1998 to 2017
$8.8M
THYROID HORMONE RECEPTORS--REGULATION AND FUNCTIONR01DK043806 · NIDDK · UNIVERSITY OF PENNSYLVANIA · PI MITCHELL A. LAZAR · 1991 to 2026
$4.9M
NIDDK NIH HHS DK19525NIDDK NIH HHS DK43806NIDDK NIH HHS DK45586NIDDK NIH HHS P30 DK019525NIDDK NIH HHS R01 DK043806NIDDK NIH HHS R01 DK045586NIDDK NIH HHS R37 DK043806
6 · The paper itself

Abstract

Nuclear receptor corepressors SMRT (silencing mediator of retinoid and thyroid receptors) and N-CoR (nuclear receptor corepressor) recruit histone deacetylase (HDAC) activity to targeted regions of chromatin. These corepressors contain a closely spaced pair of SANT motifs whose sequence and organization is highly conserved. The N-terminal SANT is a critical component of a deacetylase activation domain (DAD) that binds and activates HDAC3. Here, we show that the second SANT motif functions as part of a histone interaction domain (HID). The HID enhances repression by increasing the affinity of the DAD-HDAC3 enzyme for histone substrate. The two SANT motifs synergistically promote histone deacetylation and repression through unique functions. The HID contribution to repression is magnified by its ability to inhibit histone acetyltransferase enzyme activity. Remarkably, the SANT-containing HID preferentially binds to unacetylated histone tails. This implies that the SMRT HID participates in interpreting the histone code in a feed-forward mechanism that promotes and maintains histone deacetylation at genomic sites of SMRT recruitment.

Indexed as

AcetylationAmino Acid MotifsBase SequenceCell LineDNA-Binding ProteinsDNA PrimersHistonesHumansNuclear Receptor Co-Repressor 2Protein BindingRepressor ProteinsDNA-Binding ProteinsDNA PrimersHistonesNCOR2 protein, humanNuclear Receptor Co-Repressor 2Repressor Proteins

Identifiers

PMID12840002
PMCPMC165650
OpenAlexW2110328765

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.