2023年7月17日 · At a cellular level, H3K36M facilitates epithelial plasticity by rendering fibroblasts insensitive to TGFβ signals. At a molecular level, H3K36M enables the decommissioning of mesenchymal...

2022年11月1日 · In this review, we focus on how the histone PTM H3K36me3, the associated methyltransferase SET domain containing 2 (Set2 in yeast) and SETD2 (in mammals), the de-methylases Lysine (K)- Specific De-Methylase 4A-C (KDM4A-C), and readers of H3K36 methylation maintain genome stability.

There are diverse clues showing H3K36me3 participates in DNA damage response by directly recruiting DNA repair machinery to set the chromatin at a “ready” status, leading to a quick response upon damage. Reduced H3K36me3 is associated with low DNA repair efficiency.

2019年3月13日 · Here we report that histone H3 trimethylation at Lys36 (H3K36me3), a marker for transcription elongation, guides m 6 A deposition globally. We show that m 6 A modifications are enriched in...

We propose that H3K36me3 is a promising target for epigenetic therapeutics in cancer. H3K36me3 usually enriches active transcriptional protein-coding genes and increases in a 5′–3′ direction towards the ends of transcriptional regions [7 – 9].

2022年5月18日 · The identification of specific structural features and various cis-acting factors that bind to different forms of H3K36me, particularly the di-(H3K36me2) and tri-(H3K36me3) methylated forms of H3K36, have highlighted the intricacy of H3K36me functional significance.

2022年6月9日 · Through screening, we identify SMYD5, which is recruited to chromatin by RNA polymerase II, as a methyltransferase catalyzing H3K36me3 at promoters. The enzymatic activity of SMYD5 is dependent...

2021年10月29日 · Here we review H3K36me3-mediated biological processes and summarize the latest findings regarding its role in cancers. We highlight the significance of epigenetic combination therapies in cancers.

2020年1月8日 · Post-translational methylation of H3 lysine 36 (H3K36) is an important epigenetic marker that majorly contributes to the functionality of the chromatin. This mark is interpreted by the cell in several crucial biological processes including gene transcription and DNA methylation.

Here, we show that an epigenetic histone mark, H3K36me3, is required in vivo to recruit the mismatch recognition protein hMutSα (hMSH2-hMSH6) onto chromatin through direct interactions with the hMSH6 PWWP domain.