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Article

Cancer-driving H3G34V/R/D mutations block H3K36 methylation and H3K36me3-MutSα interaction.

Proceedings of the National Academy of Sciences of the United States of America - 18 Sept 2018

Fang Jun, Huang Yaping, Mao Guogen, Yang Shuang, Rennert Gadi, Gu Liya, Li Haitao, Li Guo-Min

Abstract excerpt

Somatic mutations on glycine 34 of histone H3 (H3G34) cause pediatric cancers, but the underlying oncogenic mechanism remains unknown. We demonstrate that substituting H3G34 with arginine, valine, or aspartate (H3G34R/V/D), which converts the non-side chain glycine to a large side chain-containing residue, blocks H3 lysine 36 (H3K36) dimethylation and trimethylation by histone methyltransferases, including SETD2,...

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Identifiers

PMID: 30181289
DOI: 10.1073/pnas.1806355115
PMCID: PMC6156674

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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