Evidence map›Paper›PMID 28341773›Full record

ArticleGenome research2017

PML protein organizes heterochromatin domains where it regulates histone H3.3 deposition by ATRX/DAXX.

Erwan Delbarre, Kristina Ivanauskiene, Jane Spirkoski, Akshay Shah, Kristin Vekterud, Jan Øivind Moskaug, Stig Ove Bøe, Lee H Wong, Thomas Küntziger, Philippe Collas

Abstract read
In one paragraph

Article in Genome research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing 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

41 citing papers in PubMed.

  1. Article
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  6. Article
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  9. Review
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  11. Review
  12. Mutant ATRX: pathogenesis of ATRX syndrome and cancer.Frontiers in molecular biosciences · 2024
    Review
  13. Article
  14. Article
  15. Article
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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

10 authors.

Erwan DelbarreDepartment of Molecular Medicine, Institute of Basic Medical Sciences, University of Oslo, 0317 Oslo, Norway.
Kristina IvanauskieneDepartment of Molecular Medicine, Institute of Basic Medical Sciences, University of Oslo, 0317 Oslo, Norway.
Jane SpirkoskiDepartment of Molecular Medicine, Institute of Basic Medical Sciences, University of Oslo, 0317 Oslo, Norway.
Akshay ShahDepartment of Molecular Medicine, Institute of Basic Medical Sciences, University of Oslo, 0317 Oslo, Norway.
Kristin VekterudDepartment of Molecular Medicine, Institute of Basic Medical Sciences, University of Oslo, 0317 Oslo, Norway.
Jan Øivind MoskaugDepartment of Molecular Medicine, Institute of Basic Medical Sciences, University of Oslo, 0317 Oslo, Norway.
Stig Ove BøeDepartment of Medical Biochemistry, Oslo University Hospital, 0027 Oslo, Norway.
Lee H WongDepartment of Biochemistry and Molecular Biology, School of Biomedical Science, Monash University, Clayton, Victoria 3800, Australia.
Thomas KüntzigerDepartment of Oral Biology, University of Oslo, 0316 Oslo, Norway.
Philippe CollasDepartment of Molecular Medicine, Institute of Basic Medical Sciences, University of Oslo, 0317 Oslo, Norway.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Maintenance of chromatin homeostasis involves proper delivery of histone variants to the genome. The interplay between different chaperones regulating the supply of histone variants to distinct chromatin domains remains largely undeciphered. We report a role of promyelocytic leukemia (PML) protein in the routing of histone variant H3.3 to chromatin and in the organization of megabase-size heterochromatic PML-associated domains that we call PADs. Loss of PML alters the heterochromatic state of PADs by shifting the histone H3 methylation balance from K9me3 to K27me3. Loss of PML impairs deposition of H3.3 by ATRX and DAXX in PADs but preserves the H3.3 loading function of HIRA in these regions. Our results unveil an unappreciated role of PML in the large-scale organization of chromatin and demonstrate a PML-dependent role of ATRX/DAXX in the deposition of H3.3 in PADs. Our data suggest that H3.3 loading by HIRA and ATRX-dependent H3K27 trimethylation constitute mechanisms ensuring maintenance of heterochromatin when the integrity of these domains is compromised.

Indexed as

AnimalsCarrier ProteinsChromatin Assembly and DisassemblyCo-Repressor ProteinsFibroblastsFluorescence Recovery After PhotobleachingGene Expression RegulationHeterochromatinHistonesIntracellular Signaling Peptides and ProteinsMethylationMiceMice, Inbred C57BLMice, KnockoutMolecular ChaperonesNuclear ProteinsAtrx protein, mouseCarrier ProteinsCo-Repressor ProteinsDaxx protein, mouseHeterochromatinHistonesIntracellular Signaling Peptides and ProteinsMolecular ChaperonesNuclear ProteinsNucleosomesPml protein, mousePromyelocytic Leukemia ProteinX-linked Nuclear Protein

Identifiers

PMID28341773
PMCPMC5453325

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Registered trials

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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.