Abstract:
: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.
journal_name
Oncogenejournal_title
Oncogeneauthors
Li Z,Jiao X,Di Sante G,Ertel A,Casimiro MC,Wang M,Katiyar S,Ju X,Klopfenstein DV,Tozeren A,Dampier W,Chepelev I,Jeltsch A,Pestell RGdoi
10.1038/s41388-019-0723-8subject
Has Abstractpub_date
2019-05-01 00:00:00pages
4232-4249issue
22eissn
0950-9232issn
1476-5594pii
10.1038/s41388-019-0723-8journal_volume
38pub_type
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