Evidence map›Paper›PMID 26055705›Full record

ArticleThe Journal of biological chemistry2015

Insights into the Recruitment of Class IIa Histone Deacetylases (HDACs) to the SMRT/NCoR Transcriptional Repression Complex.

Gregg M Hudson, Peter J Watson, Louise Fairall, Andrew G Jamieson, John W R Schwabe

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

31 citing papers in PubMed, 56 citations in OpenAlex.

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  15. HDAC3 deacetylates the DNA mismatch repair factor MutSβ to stimulate triplet repeat expansions.Proceedings of the National Academy of Sciences of the United States of America · 2020
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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

5 authors at 1 institution in 1 country.

Gregg M HudsonDepartment of Biochemistry, Henry Wellcome Laboratories of Structural Biology, University of Leicester, Leicester LE1 9HN.
Peter J WatsonDepartment of Biochemistry, Henry Wellcome Laboratories of Structural Biology, University of Leicester, Leicester LE1 9HN.
Louise FairallDepartment of Biochemistry, Henry Wellcome Laboratories of Structural Biology, University of Leicester, Leicester LE1 9HN.
Andrew G JamiesonDepartment of Chemistry, University of Leicester, Leicester LE1 7RH, United Kingdom.
John W R SchwabeDepartment of Biochemistry, Henry Wellcome Laboratories of Structural Biology, University of Leicester, Leicester LE1 9HN. Electronic address: john.schwabe@le.ac.uk.
University of Leicester · GB

Funding

Medical Research Council MC_PC_14117Wellcome Trust 085408Wellcome Trust 100237Wellcome Trust 100237/Z/12/Z
6 · The paper itself

Abstract

Class IIa histone deacetylases repress transcription of target genes. However, their mechanism of action is poorly understood because they exhibit very low levels of deacetylase activity. The class IIa HDACs are associated with the SMRT/NCoR repression complexes and this may, at least in part, account for their repressive activity. However, the molecular mechanism of recruitment to co-repressor proteins has yet to be established. Here we show that a repeated peptide motif present in both SMRT and NCoR is sufficient to mediate specific interaction, with micromolar affinity, with all the class IIa HDACs (HDACs 4, 5, 7, and 9). Mutations in the consensus motif abrogate binding. Mutational analysis of HDAC4 suggests that the peptide interacts in the vicinity of the active site of the enzyme and requires the "closed" conformation of the zinc-binding loop on the surface of the enzyme. Together these findings represent the first insights into the molecular mechanism of recruitment of class IIa HDACs to the SMRT/NCoR repression complexes.

Indexed as

Amino Acid SequenceCatalytic DomainHistone DeacetylasesHumansModels, MolecularMolecular Sequence DataNuclear Receptor Co-Repressor 2Protein Interaction Domains and MotifsProtein Interaction MapsRepressor ProteinsHDAC4 protein, humanHistone DeacetylasesNCOR2 protein, humanNuclear Receptor Co-Repressor 2Repressor Proteinsepigeneticshistone acetylationhistone deacetylase 4 (HDAC4)protein-protein interactiontranscription corepressor

Identifiers

PMID26055705
PMCPMC4505066
OpenAlexW1479760774

What OpenQuestion holds

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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.