Evidence map›Paper›PMID 38403935›Full record

ArticleGenes to cells : devoted to molecular & cellular mechanisms2024

Mode of SUV420H2 heterochromatin localization through multiple HP1 binding motifs in the heterochromatic targeting module.

Masaru Nakao, Yuko Sato, Arisa Aizawa, Hiroshi Kimura

Open access · hybridAbstract read
In one paragraph

Article in Genes to cells : devoted to molecular & cellular mechanisms, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
1.6field-weighted citation impact, top 18% 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

4 citing papers in PubMed, 7 citations in OpenAlex.

  1. Article
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  3. Review
  4. 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

4 authors at 1 institution in 2 countries.

Masaru NakaoSchool of Life Science and Technology, Tokyo Institute of Technology, Yokohama, Japan.
Yuko SatoSchool of Life Science and Technology, Tokyo Institute of Technology, Yokohama, Japan.ORCID https://orcid.org/0000-0002-7805-9171
Arisa AizawaSchool of Life Science and Technology, Tokyo Institute of Technology, Yokohama, Japan.
Hiroshi KimuraSchool of Life Science and Technology, Tokyo Institute of Technology, Yokohama, Japan.ORCID https://orcid.org/0000-0003-0854-083X
Tokyo Institute of Technology · JP

Funding

Core Research for Evolutional Science and Technology JPMJCR16G1Core Research for Evolutional Science and Technology JPMJCR20S6Japan Agency for Medical Research and Development JP23ama121020Japan Society for the Promotion of Science JP17H01417Japan Society for the Promotion of Science JP21H04764
6 · The paper itself

Abstract

Constitutive heterochromatin is transcriptionally repressed and densely packed chromatin, typically harboring histone H3 Lys9 trimethylation (H3K9me3) and heterochromatin protein 1 (HP1). SUV420H2, a histone H4 Lys20 methyltransferase, is recruited to heterochromatin by binding to HP1 through its Heterochromatic Targeting Module (HTM). Here, we have identified three HP1 binding motifs within the HTM. Both the full-length HTM and its N-terminal region (HTM-N), which contains the first and second motifs, stabilized HP1 on heterochromatin. The intervening region between the first and second HP1 binding motifs in HTM-N was also crucial for HP1 binding. In contrast, the C-terminal region of HTM (HTM-C), containing the third motif, destabilized HP1 on chromatin. An HTM V374D mutant, featuring a Val374 to Asp substitution in the second HP1 binding motif, localizes to heterochromatin without affecting HP1 stability. These data suggest that the second HP1 binding motif in the SUV420H2 HTM is critical for locking HP1 on H3K9me3-enriched heterochromatin. HTM V374D, tagged with a fluorescent protein, can serve as a live-cell probe to visualize HP1-bound heterochromatin.

Indexed as

Chromobox Protein Homolog 5Chromosomal Proteins, Non-HistoneHeterochromatinHistone-Lysine N-MethyltransferaseProtein BindingAmino Acid MotifsBinding SitesHeLa CellsHistonesHumansChromobox Protein Homolog 5Chromosomal Proteins, Non-HistoneHeterochromatinHistone-Lysine N-MethyltransferaseHistonesKMT5C protein, humanchromatinepigeneticsH3K9me3H4K20me3heterochromatinHP1SUV420H2

Identifiers

PMID38403935
PMCPMC11163940
OpenAlexW4392167255

What OpenQuestion holds

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LicenceCC BY-NC
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.