Evidence map›Paper›PMID 30321390›Full record

ArticleNucleic acids research2018

Structural basis of the specific interaction of SMRT corepressor with histone deacetylase 4.

Suk-Youl Park, Gwang Sik Kim, Hyo-Jeong Hwang, Taek-Hyun Nam, Hee-Sae Park, Jaeyoung Song, Tae-Ho Jang, Young Chul Lee, Jeong-Sun Kim

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.0field-weighted citation impact, top 24% 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

19 citing papers in PubMed, 34 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Selective HDAC4 inhibition by SP1-PTD promotes odontoblast differentiation.Journal of applied oral science : revista FOB · 2025
    Article
  6. Review
  7. Review
  8. HDAC-driven mechanisms in anticancer resistance: epigenetics and beyond.Cancer drug resistance (Alhambra, Calif.) · 2024
    Review
  9. Article
  10. Article
  11. Review
  12. Review
  13. Article
  14. Article
  15. Article
  16. Review
  17. Review
  18. Review
  19. 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

9 authors at 2 institutions in 1 country.

Suk-Youl ParkDepartment of Chemistry, Chonnam National University, Gwangju 61186, Republic of Korea.
Gwang Sik KimSchool of Biological Sciences and Technology, Chonnam National University, Gwangju 61186, Republic of Korea.
Hyo-Jeong HwangDepartment of Chemistry, Chonnam National University, Gwangju 61186, Republic of Korea.
Taek-Hyun NamSchool of Biological Sciences and Technology, Chonnam National University, Gwangju 61186, Republic of Korea.
Hee-Sae ParkSchool of Biological Sciences and Technology, Chonnam National University, Gwangju 61186, Republic of Korea.
Jaeyoung SongNew Drug Development Center, Daegu-Gyeongbuk Medical Innovation Foundation, Daegu 41061, Republic of Korea.
Tae-Ho JangNew Drug Development Center, Daegu-Gyeongbuk Medical Innovation Foundation, Daegu 41061, Republic of Korea.
Young Chul LeeSchool of Biological Sciences and Technology, Chonnam National University, Gwangju 61186, Republic of Korea.
Jeong-Sun KimDepartment of Chemistry, Chonnam National University, Gwangju 61186, Republic of Korea.
Chonnam National University · KRDaegu-Gyeongbuk Medical Innovation Foundation · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Modification of chromatin and related transcription factors by histone deacetylases (HDACs) is one of the major strategies for controlling gene expression in eukaryotes. The HDAC domains of class IIa HDACs repress the respective target genes by interacting with the C-terminal region of the silencing mediator for retinoid and thyroid receptor (SMRT) repression domain 3 (SRD3c). However, latent catalytic activity suggests that their roles as deacetylases in gene regulation are unclear. Here, we found that two conserved GSI-containing motifs of SRD3c are critical for HDAC4 binding. Two SMRT peptides including these motifs commonly form a β-hairpin structure in the cleft and block the catalytic entry site of HDAC4. They interact mainly with class IIa HDAC-specific residues of HDAC4 in a closed conformation. Structure-guided mutagenesis confirmed critical interactions between the SMRT peptides and HDAC4 and -5 as well as the contribution of the Arg1369 residue in the first motif for optimal binding to the two HDACs. These results indicate that SMRT binding does not activate the cryptic deacetylase activity of HDAC4 and explain how class IIa HDACs and the SMRT-HDAC3 complex are coordinated during gene regulation.

Indexed as

Amino Acid MotifsArginineCatalytic DomainHEK293 CellsHistone DeacetylasesHumansMicroscopy, ConfocalMutagenesisMutagenesis, Site-DirectedMutationNuclear Receptor Co-Repressor 2PeptidesProtein BindingRepressor ProteinsThermodynamicsArginineHDAC4 protein, humanHDAC5 protein, humanHistone DeacetylasesNuclear Receptor Co-Repressor 2PeptidesRepressor Proteins

Identifiers

PMID30321390
PMCPMC6294515
OpenAlexW2896021495

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.