Evidence map›Paper›PMID 32591534›Full record

ArticleNature communications2020

The MiDAC histone deacetylase complex is essential for embryonic development and has a unique multivalent structure.

Robert E Turnbull, Louise Fairall, Almutasem Saleh, Emma Kelsall, Kyle L Morris, T J Ragan, Christos G Savva, Aditya Chandru, Christopher J Millard, Olga V Makarova and 5 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.

0numbers the graph read from it
0cells of the map it votes in
52citing papers in PubMed
6.2field-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

52 citing papers in PubMed, 108 citations in OpenAlex.

  1. Article
  2. Review
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  4. Review
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  8. Article
  9. Complex-specific HDAC1/2 regulation in the heart: insights from MiDAC disruption.American journal of physiology. Heart and circulatory physiology · 2026
    Article
  10. Article
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  14. Loss of Elmsan1 in cardiomyocytes leads to age-dependent cardiac dysfunction and reduced lifespan.American journal of physiology. Heart and circulatory physiology · 2025
    Article
  15. Review
  16. Article
  17. Circular Engineered Sortase for Interrogating Histone H3 in Chromatin.Journal of the American Chemical Society · 2024
    Article
  18. A circular engineered sortase for interrogating histone H3 in chromatin.bioRxiv : the preprint server for biology · 2024
    Article
  19. Article
  20. 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

15 authors at 4 institutions in 2 countries.

Robert E Turnbull *Leicester Institute of Structural and Chemical Biology, University of Leicester, Leicester, LE1 7RH, UK.ORCID http://orcid.org/0000-0003-2863-4374
Louise Fairall *Leicester Institute of Structural and Chemical Biology, University of Leicester, Leicester, LE1 7RH, UK.
Almutasem Saleh *Leicester Institute of Structural and Chemical Biology, University of Leicester, Leicester, LE1 7RH, UK.
Emma Kelsall *Department of Molecular and Cell Biology, University of Leicester, Leicester, LE1 7RH, UK.
Kyle L MorrisSchool of Life Sciences, University of Warwick, Coventry, CV4 7AL, UK.
T J RaganLeicester Institute of Structural and Chemical Biology, University of Leicester, Leicester, LE1 7RH, UK.ORCID http://orcid.org/0000-0002-6233-3375
Christos G SavvaLeicester Institute of Structural and Chemical Biology, University of Leicester, Leicester, LE1 7RH, UK.
Aditya ChandruDepartment of Molecular and Cell Biology, University of Leicester, Leicester, LE1 7RH, UK.
Christopher J MillardLeicester Institute of Structural and Chemical Biology, University of Leicester, Leicester, LE1 7RH, UK.ORCID http://orcid.org/0000-0002-1012-0829
Olga V MakarovaDepartment of Molecular and Cell Biology, University of Leicester, Leicester, LE1 7RH, UK.
Corinne J SmithSchool of Life Sciences, University of Warwick, Coventry, CV4 7AL, UK.ORCID http://orcid.org/0000-0003-3364-7946
Alan M RosemanDivision of Molecular and Cellular Function, University of Manchester, Manchester, M13 9PL, UK.
Andrew M FryDepartment of Molecular and Cell Biology, University of Leicester, Leicester, LE1 7RH, UK.
Shaun M CowleyDepartment of Molecular and Cell Biology, University of Leicester, Leicester, LE1 7RH, UK. smc57@leicester.ac.uk.ORCID http://orcid.org/0000-0002-2510-1305
John W R SchwabeLeicester Institute of Structural and Chemical Biology, University of Leicester, Leicester, LE1 7RH, UK. john.schwabe@leicester.ac.uk.ORCID http://orcid.org/0000-0003-2865-4383
University of Leicester · GBHammersmith Hospital · GBUniversity of Manchester · GBUniversity of Warwick · GB

Funding

Biotechnology and Biological Sciences Research Council BB/N002954/1Medical Research Council MC_PC_17136Medical Research Council MR/J009202/1Wellcome Trust 055663/Z/98/ZWellcome Trust 100237Wellcome Trust 100237/Z/12/Z
6 · The paper itself

Abstract

MiDAC is one of seven distinct, large multi-protein complexes that recruit class I histone deacetylases to the genome to regulate gene expression. Despite implications of involvement in cell cycle regulation and in several cancers, surprisingly little is known about the function or structure of MiDAC. Here we show that MiDAC is important for chromosome alignment during mitosis in cancer cell lines. Mice lacking the MiDAC proteins, DNTTIP1 or MIDEAS, die with identical phenotypes during late embryogenesis due to perturbations in gene expression that result in heart malformation and haematopoietic failure. This suggests that MiDAC has an essential and unique function that cannot be compensated by other HDAC complexes. Consistent with this, the cryoEM structure of MiDAC reveals a unique and distinctive mode of assembly. Four copies of HDAC1 are positioned at the periphery with outward-facing active sites suggesting that the complex may target multiple nucleosomes implying a processive deacetylase function.

Indexed as

Embryonic DevelopmentAmino Acid SequenceAnimalsCell LineChromatinChromosomes, MammalianEmbryo, MammalianFibroblastsGene Regulatory NetworksHeterozygoteHistone DeacetylasesHomozygoteHumansMice, Inbred C57BLMice, KnockoutMitosisChromatinHistone DeacetylasesMultiprotein ComplexesNuclear Proteins

Identifiers

PMID32591534
PMCPMC7319964
OpenAlexW3037025246

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.