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Cyclin D1 integrates G9a-mediated histone methylation
Journal article   Open access   Peer reviewed

Cyclin D1 integrates G9a-mediated histone methylation

Zhiping Li, Xuanmao Jiao, Gabriele Di Sante, Adam Ertel, Mathew C Casimiro, Min Wang, Sanjay Katiyar, Xiaoming Ju, D V Klopfenstein, Aydin Tozeren, …
Oncogene, v 38(22), pp 4232-4249
May 2019
DOI: https://doi.org/10.1038/s41388-019-0723-8
PMID: 30718920
Featured in Collection :   UN Sustainable Development Goals @ Drexel
url
https://doi.org/10.1038/s41388-019-0723-8View
Published, Version of Record (VoR)CC BY V4.0,  Open

Abstract

Cell Cycle - physiology Cell Line Cell Line, Tumor Chromatin - metabolism Chromosomes - physiology Cyclin D1 - metabolism DNA Methylation - physiology HEK293 Cells Histocompatibility Antigens - metabolism Histone-Lysine N-Methyltransferase - metabolism Histones - metabolism Humans MCF-7 Cells Protein Binding - physiology
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.

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Collaboration types
Domestic collaboration
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Web of Science research areas
Biochemistry & Molecular Biology
Cell Biology
Genetics & Heredity
Oncology
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