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Cyclin D1 integrates G9a-mediated histone methylation
Lysine methylation of histones and non-histone substrates by the SET domain containing protein lysine methyltransferase (KMT) G9a/EHMT2 governs transcription contributing to apoptosis, aberrant cell growth, and pluripotency. The positioning of chromosomes within the nuclear three-dimensional space i...
Autores principales: | , , , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6542714/ https://www.ncbi.nlm.nih.gov/pubmed/30718920 http://dx.doi.org/10.1038/s41388-019-0723-8 |
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author | Li, Zhiping Jiao, Xuanmao Di Sante, Gabriele Ertel, Adam Casimiro, Mathew C. Wang, Min Katiyar, Sanjay Ju, Xiaoming Klopfenstein, D. V. Tozeren, Aydin Dampier, William Chepelev, Iouri Jeltsch, Albert Pestell, Richard G. |
author_facet | Li, Zhiping Jiao, Xuanmao Di Sante, Gabriele Ertel, Adam Casimiro, Mathew C. Wang, Min Katiyar, Sanjay Ju, Xiaoming Klopfenstein, D. V. Tozeren, Aydin Dampier, William Chepelev, Iouri Jeltsch, Albert Pestell, Richard G. |
author_sort | Li, Zhiping |
collection | PubMed |
description | Lysine methylation of histones and non-histone substrates by the SET domain containing protein lysine methyltransferase (KMT) G9a/EHMT2 governs transcription contributing to apoptosis, aberrant cell growth, and pluripotency. The positioning of chromosomes within the nuclear three-dimensional space involves interactions between nuclear lamina (NL) and the lamina-associated domains (LAD). Contact of individual LADs with the NL are dependent upon H3K9me2 introduced by G9a. The mechanisms governing the recruitment of G9a to distinct subcellular sites, into chromatin or to LAD, is not known. The cyclin D1 gene product encodes the regulatory subunit of the holoenzyme that phosphorylates pRB and NRF1 thereby governing cell-cycle progression and mitochondrial metabolism. Herein, we show that cyclin D1 enhanced H3K9 dimethylation though direct association with G9a. Endogenous cyclin D1 was required for the recruitment of G9a to target genes in chromatin, for G9a-induced H3K9me2 of histones, and for NL-LAD interaction. The finding that cyclin D1 is required for recruitment of G9a to target genes in chromatin and for H3K9 dimethylation, identifies a novel mechanism coordinating protein methylation. |
format | Online Article Text |
id | pubmed-6542714 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-65427142019-08-04 Cyclin D1 integrates G9a-mediated histone methylation Li, Zhiping Jiao, Xuanmao Di Sante, Gabriele Ertel, Adam Casimiro, Mathew C. Wang, Min Katiyar, Sanjay Ju, Xiaoming Klopfenstein, D. V. Tozeren, Aydin Dampier, William Chepelev, Iouri Jeltsch, Albert Pestell, Richard G. Oncogene Article Lysine methylation of histones and non-histone substrates by the SET domain containing protein lysine methyltransferase (KMT) G9a/EHMT2 governs transcription contributing to apoptosis, aberrant cell growth, and pluripotency. The positioning of chromosomes within the nuclear three-dimensional space involves interactions between nuclear lamina (NL) and the lamina-associated domains (LAD). Contact of individual LADs with the NL are dependent upon H3K9me2 introduced by G9a. The mechanisms governing the recruitment of G9a to distinct subcellular sites, into chromatin or to LAD, is not known. The cyclin D1 gene product encodes the regulatory subunit of the holoenzyme that phosphorylates pRB and NRF1 thereby governing cell-cycle progression and mitochondrial metabolism. Herein, we show that cyclin D1 enhanced H3K9 dimethylation though direct association with G9a. Endogenous cyclin D1 was required for the recruitment of G9a to target genes in chromatin, for G9a-induced H3K9me2 of histones, and for NL-LAD interaction. The finding that cyclin D1 is required for recruitment of G9a to target genes in chromatin and for H3K9 dimethylation, identifies a novel mechanism coordinating protein methylation. Nature Publishing Group UK 2019-02-04 2019 /pmc/articles/PMC6542714/ /pubmed/30718920 http://dx.doi.org/10.1038/s41388-019-0723-8 Text en © The Author(s) 2019 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/. |
spellingShingle | Article Li, Zhiping Jiao, Xuanmao Di Sante, Gabriele Ertel, Adam Casimiro, Mathew C. Wang, Min Katiyar, Sanjay Ju, Xiaoming Klopfenstein, D. V. Tozeren, Aydin Dampier, William Chepelev, Iouri Jeltsch, Albert Pestell, Richard G. Cyclin D1 integrates G9a-mediated histone methylation |
title | Cyclin D1 integrates G9a-mediated histone methylation |
title_full | Cyclin D1 integrates G9a-mediated histone methylation |
title_fullStr | Cyclin D1 integrates G9a-mediated histone methylation |
title_full_unstemmed | Cyclin D1 integrates G9a-mediated histone methylation |
title_short | Cyclin D1 integrates G9a-mediated histone methylation |
title_sort | cyclin d1 integrates g9a-mediated histone methylation |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6542714/ https://www.ncbi.nlm.nih.gov/pubmed/30718920 http://dx.doi.org/10.1038/s41388-019-0723-8 |
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