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H3S28 phosphorylation is a hallmark of the transcriptional response to cellular stress
The selectivity of transcriptional responses to extracellular cues is reflected by the deposition of stimulus-specific chromatin marks. Although histone H3 phosphorylation is a target of numerous signaling pathways, its role in transcriptional regulation remains poorly understood. Here, for the firs...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Cold Spring Harbor Laboratory Press
2014
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4216922/ https://www.ncbi.nlm.nih.gov/pubmed/25135956 http://dx.doi.org/10.1101/gr.176255.114 |
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author | Sawicka, Anna Hartl, Dominik Goiser, Malgorzata Pusch, Oliver Stocsits, Roman R. Tamir, Ido M. Mechtler, Karl Seiser, Christian |
author_facet | Sawicka, Anna Hartl, Dominik Goiser, Malgorzata Pusch, Oliver Stocsits, Roman R. Tamir, Ido M. Mechtler, Karl Seiser, Christian |
author_sort | Sawicka, Anna |
collection | PubMed |
description | The selectivity of transcriptional responses to extracellular cues is reflected by the deposition of stimulus-specific chromatin marks. Although histone H3 phosphorylation is a target of numerous signaling pathways, its role in transcriptional regulation remains poorly understood. Here, for the first time, we report a genome-wide analysis of H3S28 phosphorylation in a mammalian system in the context of stress signaling. We found that this mark targets as many as 50% of all stress-induced genes, underlining its importance in signal-induced transcription. By combining ChIP-seq, RNA-seq, and mass spectrometry we identified the factors involved in the biological interpretation of this histone modification. We found that MSK1/2-mediated phosphorylation of H3S28 at stress-responsive promoters contributes to the dissociation of HDAC corepressor complexes and thereby to enhanced local histone acetylation and subsequent transcriptional activation of stress-induced genes. Our data reveal a novel function of the H3S28ph mark in the activation of mammalian genes in response to MAP kinase pathway activation. |
format | Online Article Text |
id | pubmed-4216922 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | Cold Spring Harbor Laboratory Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-42169222014-11-04 H3S28 phosphorylation is a hallmark of the transcriptional response to cellular stress Sawicka, Anna Hartl, Dominik Goiser, Malgorzata Pusch, Oliver Stocsits, Roman R. Tamir, Ido M. Mechtler, Karl Seiser, Christian Genome Res Research The selectivity of transcriptional responses to extracellular cues is reflected by the deposition of stimulus-specific chromatin marks. Although histone H3 phosphorylation is a target of numerous signaling pathways, its role in transcriptional regulation remains poorly understood. Here, for the first time, we report a genome-wide analysis of H3S28 phosphorylation in a mammalian system in the context of stress signaling. We found that this mark targets as many as 50% of all stress-induced genes, underlining its importance in signal-induced transcription. By combining ChIP-seq, RNA-seq, and mass spectrometry we identified the factors involved in the biological interpretation of this histone modification. We found that MSK1/2-mediated phosphorylation of H3S28 at stress-responsive promoters contributes to the dissociation of HDAC corepressor complexes and thereby to enhanced local histone acetylation and subsequent transcriptional activation of stress-induced genes. Our data reveal a novel function of the H3S28ph mark in the activation of mammalian genes in response to MAP kinase pathway activation. Cold Spring Harbor Laboratory Press 2014-11 /pmc/articles/PMC4216922/ /pubmed/25135956 http://dx.doi.org/10.1101/gr.176255.114 Text en © 2014 Sawicka et al.; Published by Cold Spring Harbor Laboratory Press http://creativecommons.org/licenses/by/4.0/ This article, published in Genome Research, is available under a Creative Commons License (Attribution 4.0 International), as described at http://creativecommons.org/licenses/by/4.0. |
spellingShingle | Research Sawicka, Anna Hartl, Dominik Goiser, Malgorzata Pusch, Oliver Stocsits, Roman R. Tamir, Ido M. Mechtler, Karl Seiser, Christian H3S28 phosphorylation is a hallmark of the transcriptional response to cellular stress |
title | H3S28 phosphorylation is a hallmark of the transcriptional response to cellular stress |
title_full | H3S28 phosphorylation is a hallmark of the transcriptional response to cellular stress |
title_fullStr | H3S28 phosphorylation is a hallmark of the transcriptional response to cellular stress |
title_full_unstemmed | H3S28 phosphorylation is a hallmark of the transcriptional response to cellular stress |
title_short | H3S28 phosphorylation is a hallmark of the transcriptional response to cellular stress |
title_sort | h3s28 phosphorylation is a hallmark of the transcriptional response to cellular stress |
topic | Research |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4216922/ https://www.ncbi.nlm.nih.gov/pubmed/25135956 http://dx.doi.org/10.1101/gr.176255.114 |
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