ArticleEpigenetics2011
HP1α is not necessary for the structural maintenance of centromeric heterochromatin.
Article in Epigenetics, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
What it found
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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.
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.
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Who cites it
3 citing papers in PubMed, 6 citations in OpenAlex.
- Review
- Mechanisms of heat shock response in mammals.Cellular and molecular life sciences : CMLS · 2013Review
- Dualistic function of Daxx at centromeric and pericentromeric heterochromatin in normal and stress conditions.Nucleus (Austin, Tex.)Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Heterochromatin protein 1 (HP1) was discovered as a protein essential for maintaining the silent transcriptional status of genes located within or close to centromeric regions of Drosophila chromosomes. Mammals express three variants of HP1; of these, HP1α is a direct homolog of Drosophila HP1. The prevailing view states that HP1 is a structural component of heterochromatin and is essential for compact DNA packaging. HP1 contains a chromodomain that binds to di- and- tri-methylated lysine 9 of histone H3. Additionally, it contains a chromoshadow domain that allows HP1 to dimerize and interact with other proteins. HP1 is thought to form "bridges" between neighboring rows of nucleosomes in heterochromatin. In mammalian cells, a significant portion of HP1α is located in the centromeric regions of chromosomes. In this study, we show that the majority of HP1α is removed from centromeres upon heat shock. This occurs without a loss of H3K9 trimethylation and does not correlate with a decompaction of centromeres. Furthermore, HP1α is not degraded and remains bound to chromatin. Therefore, it is likely that HP1α is simply redistributed to euchromatic regions. We propose that this redistribution is essential for reversal of the transcriptional status of euchromatic and heterochromatic compartments.
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Registered trials
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