Evidence map›Paper›PMID 22247192›Full record

ArticleJournal of cell science2011

The epigenetic H3S10 phosphorylation mark is required for counteracting heterochromatic spreading and gene silencing in Drosophila melanogaster.

Chao Wang, Weili Cai, Yeran Li, Huai Deng, Xiaomin Bao, Jack Girton, Jørgen Johansen, Kristen M Johansen

Abstract read
In one paragraph

Article in Journal of cell science, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.7field-weighted citation impact, top 17% 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

16 citing papers in PubMed, 23 citations in OpenAlex.

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  6. A new player in X identification: the CLAMP protein is a key factor in Drosophila dosage compensation.Chromosome research : an international journal on the molecular, supramolecular and evolutionary aspects of chromosome biology · 2014
    Review
  7. Epigenetic dysregulation by nickel through repressive chromatin domain disruption.Proceedings of the National Academy of Sciences of the United States of America · 2014
    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

8 authors at 1 institution in 1 country.

Chao WangDepartment of Biochemistry, Biophysics and Molecular Biology, Iowa State University Ames, IA 50011, USA.
Weili Cai
Yeran Li
Huai Deng
Xiaomin Bao
Jack Girton
Jørgen Johansen
Kristen M Johansen
Iowa State University · US

Funding

Regulation of Chromatin Structure byPhosphorylationR01GM062916 · NIGMS · IOWA STATE UNIVERSITY · PI JOHANSEN, JORGEN, JOHANSEN, KRISTEN M · 2001 to 2014
$3.5M
NIGMS NIH HHS GM062916NIGMS NIH HHS R01 GM062916
6 · The paper itself

Abstract

The JIL-1 kinase localizes specifically to euchromatin interband regions of polytene chromosomes and is the kinase responsible for histone H3S10 phosphorylation at interphase. Genetic interaction assays with strong JIL-1 hypomorphic loss-of-function alleles have demonstrated that the JIL-1 protein can counterbalance the effect of the major heterochromatin components on position-effect variegation (PEV) and gene silencing. However, it is unclear whether this was a causative effect of the epigenetic H3S10 phosphorylation mark, or whether the effect of the JIL-1 protein on PEV was in fact caused by other functions or structural features of the protein. By transgenically expressing various truncated versions of JIL-1, with or without kinase activity, and assessing their effect on PEV and heterochromatic spreading, we show that the gross perturbation of polytene chromosome morphology observed in JIL-1 null mutants is unrelated to gene silencing in PEV and is likely to occur as a result of faulty polytene chromosome alignment and/or organization, separate from epigenetic regulation of chromatin structure. Furthermore, the findings provide evidence that the epigenetic H3S10 phosphorylation mark itself is necessary for preventing the observed heterochromatic spreading independently of any structural contributions from the JIL-1 protein.

Indexed as

Chromosomal Position EffectsEpigenesis, GeneticGene SilencingAnimalsDrosophila melanogasterDrosophila ProteinsEyeHeterochromatinHistonesPhosphorylationProtein Serine-Threonine KinasesProtein Structure, TertiaryTransgenesDrosophila ProteinsHeterochromatinHistonesJIL-1 protein, DrosophilaProtein Serine-Threonine Kinases

Identifiers

PMID22247192
PMCPMC3258113
OpenAlexW1968127223

What OpenQuestion holds

Textmetadata
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.