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Cyclin D1 integrates G9a-mediated histone methylation

by Tozeren, Aydin , Di Sante, Gabriele , Ju, Xiaoming , Casimiro, Mathew C. , Jiao, Xuanmao , Li, Zhiping , Katiyar, Sanjay , Jeltsch, Albert , Ertel, Adam , Pestell, Richard G. , Wang, Min , Klopfenstein, D. V. , Chepelev, Iouri , Dampier, William

in 13 / 14/19 / 38 / 38/39 / 38/89 / 631/67/1347 / 631/80/86/2371 / 82/51 / 82/80 / 96/109 / 96/35 / Apoptosis / Backup software / Cell Biology / Cell Cycle - physiology / Cell Line / Cell Line, Tumor / Chromatin / Chromatin - metabolism / Chromosomes / Chromosomes - physiology / Cyclin D1 / Cyclin D1 - metabolism / DNA binding proteins / DNA Methylation - physiology / Enzymes / HEK293 Cells / Histocompatibility Antigens - metabolism / Histone-Lysine N-Methyltransferase - metabolism / Histones / Histones - metabolism / Human Genetics / Humans / Internal Medicine / Lysine / MCF-7 Cells / Medicine / Medicine & Public Health / Methylation / Methyltransferase / Mitochondria / Novels / Oncology / Pluripotency / Protein Binding - physiology / Recruitment / Transcription / Transcription factors / Transferases

2019

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Cyclin D1 integrates G9a-mediated histone methylation

2019

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2019

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Journal Article

Cyclin D1 integrates G9a-mediated histone methylation

Tozeren, Aydin,

Di Sante, Gabriele,

Ju, Xiaoming,

Casimiro, Mathew C.,

Jiao, Xuanmao,

Li, Zhiping,

Katiyar, Sanjay,

Jeltsch, Albert,

Ertel, Adam,

Pestell, Richard G.,

Wang, Min,

Klopfenstein, D. V.,

Chepelev, Iouri,

Dampier, William

2019

Overview

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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Publisher

Nature Publishing Group UK,Nature Publishing Group

Subject

/ 14/19

/ 38

/ 38/39

/ 38/89

/ 631/67/1347

/ 631/80/86/2371

/ 82/51