Evidence map›Paper›PMID 37137925›Full record

ArticleNature communications2023

Mechanism of assembly, activation and lysine selection by the SIN3B histone deacetylase complex.

Mandy S M Wan, Reyhan Muhammad, Marios G Koliopoulos, Theodoros I Roumeliotis, Jyoti S Choudhary, Claudio Alfieri

Abstract read
In one paragraph

Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
–field-weighted citation impact
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

18 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. 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

6 authors.

Mandy S M Wan *Division of Structural Biology, Chester Beatty Laboratories, The Institute of Cancer Research, London, UK.ORCID 0000-0002-0679-4142
Reyhan Muhammad *Division of Structural Biology, Chester Beatty Laboratories, The Institute of Cancer Research, London, UK.
Marios G KoliopoulosDivision of Structural Biology, Chester Beatty Laboratories, The Institute of Cancer Research, London, UK.
Theodoros I RoumeliotisFunctional Proteomics, Chester Beatty Laboratories, Cancer Biology Division, The Institute of Cancer Research, London, UK.ORCID 0000-0002-3354-5643
Jyoti S ChoudharyFunctional Proteomics, Chester Beatty Laboratories, Cancer Biology Division, The Institute of Cancer Research, London, UK.ORCID 0000-0003-0881-5477
Claudio AlfieriDivision of Structural Biology, Chester Beatty Laboratories, The Institute of Cancer Research, London, UK. claudio.alfieri@icr.ac.uk.ORCID 0000-0003-3215-1607

Funding

Cancer Research UK (CRUK) C309/A25144Wellcome TrustWellcome Trust (Wellcome) 215458/Z/19/Z
6 · The paper itself

Abstract

Lysine acetylation in histone tails is a key post-translational modification that controls transcription activation. Histone deacetylase complexes remove histone acetylation, thereby repressing transcription and regulating the transcriptional output of each gene. Although these complexes are drug targets and crucial regulators of organismal physiology, their structure and mechanisms of action are largely unclear. Here, we present the structure of a complete human SIN3B histone deacetylase holo-complex with and without a substrate mimic. Remarkably, SIN3B encircles the deacetylase and contacts its allosteric basic patch thereby stimulating catalysis. A SIN3B loop inserts into the catalytic tunnel, rearranges to accommodate the acetyl-lysine moiety, and stabilises the substrate for specific deacetylation, which is guided by a substrate receptor subunit. Our findings provide a model of specificity for a main transcriptional regulator conserved from yeast to human and a resource of protein-protein interactions for future drug designs.

Indexed as

HistonesLysineAcetylationHistone Deacetylase 1Histone DeacetylasesHumansProtein Processing, Post-TranslationalRepressor ProteinsSaccharomyces cerevisiaeHistone Deacetylase 1Histone DeacetylasesHistonesLysineRepressor ProteinsSIN3B protein, human

Identifiers

PMID37137925
PMCPMC10156912

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.