Evidence map›Paper›PMID 26581166›Full record

ArticleScientific reports2015

Linker histone H1.2 establishes chromatin compaction and gene silencing through recognition of H3K27me3.

Jin-Man Kim, Kyunghwan Kim, Vasu Punj, Gangning Liang, Tobias S Ulmer, Wange Lu, Woojin An

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

35 citing papers in PubMed, 59 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Review
  12. Article
  13. Genetics and Epigenetics of Parathyroid Carcinoma.Frontiers in endocrinology · 2022
    Review
  14. Parathyroid Tumors: Molecular Signatures.International journal of molecular sciences · 2021
    Review
  15. Article
  16. Histone tails as signaling antennas of chromatin.Current opinion in structural biology · 2021
    Review
  17. Article
  18. Molecular and Cellular Functions of the Linker Histone H1.2.Frontiers in cell and developmental biology · 2021
    Review
  19. The missing linkGenes & development · 2021
    Review
  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

7 authors at 2 institutions in 2 countries.

Jin-Man KimDepartment of Biochemistry and Molecular Biology, University of Southern California, Los Angeles, CA 90033, USA.
Kyunghwan KimDepartment of Biochemistry and Molecular Biology, University of Southern California, Los Angeles, CA 90033, USA.
Vasu PunjNorris Comprehensive Cancer Center, University of Southern California, Los Angeles, CA 90033, USA.
Gangning LiangDepartment of Urology, Keck School of Medicine, University of Southern California, Los Angeles, CA 90033, USA.
Tobias S UlmerDepartment of Biochemistry and Molecular Biology, University of Southern California, Los Angeles, CA 90033, USA.
Wange LuDepartment of Biochemistry and Molecular Biology, University of Southern California, Los Angeles, CA 90033, USA.
Woojin AnDepartment of Biochemistry and Molecular Biology, University of Southern California, Los Angeles, CA 90033, USA.
University of Southern California · USChungbuk National University · KR

Funding

ROLE OF HISTONE H4 N-TERMINAL TAIL IN TRANSCRIPTION REGULATIONR01GM084209 · NIGMS · UNIVERSITY OF SOUTHERN CALIFORNIA · PI AN, WOOJIN · 2008 to 2012
$1.8M
NIGMS NIH HHS GM84209NIGMS NIH HHS R01 GM084209
6 · The paper itself

Abstract

Linker histone H1 is a protein component of chromatin and has been linked to higher-order chromatin compaction and global gene silencing. However, a growing body of evidence suggests that H1 plays a gene-specific role, regulating a relatively small number of genes. Here we show that H1.2, one of the H1 subtypes, is overexpressed in cancer cells and contributes to gene silencing. H1.2 gets recruited to distinct chromatin regions in a manner dependent on EZH2-mediated H3K27me3, and inhibits transcription of multiple growth suppressive genes via modulation of chromatin architecture. The C-terminal tail of H1.2 is critical for the observed effects, because mutations of three H1.2-specific amino acids in this domain abrogate the ability of H1.2 to bind H3K27me3 nucleosomes and inactivate target genes. Collectively, these results provide a molecular explanation for H1.2 functions in the regulation of chromatin folding and indicate that H3K27me3 is a key mechanism governing the recruitment and activity of H1.2 at target loci.

Indexed as

Gene SilencingCell Line, TumorCell ProliferationChromatinEnhancer of Zeste Homolog 2 ProteinGenetic LociHistonesHumansLysineMethylationNucleosomesPolycomb Repressive Complex 2Protein BindingTranscription, GeneticChromatinEnhancer of Zeste Homolog 2 ProteinEZH2 protein, humanHistonesLysineNucleosomesPolycomb Repressive Complex 2

Identifiers

PMID26581166
PMCPMC4652225
OpenAlexW2419037911

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.