Smyd3 regulates cancer cell phenotypes and catalyzes histone H4 lysine 5 methylation

• Published in: Epigenetics Vol. 7; no. 4; pp. 340 - 343
• Main Authors: Van Aller, Glenn S, Reynoird, Nicolas, Barbash, Olena, Huddleston, Michael, Liu, Shichong, Zmoos, Anne-Flore, McDevitt, Patrick, Sinnamon, Robert, Le, BaoChau, Mas, Gloria, Annan, Roland, Sage, Julien, Garcia, Benjamin A, Tummino, Peter J, Gozani, Or, Kruger, Ryan G
• Format: Journal Article
• Language: English
• Published: United States Taylor & Francis 01.04.2012; Landes Bioscience
• Subjects: Animals; Binding; Biology; Bioscience; Blotting, Western; Brief Report; Calcium; Cancer; Cell; Chromatin - genetics; Chromatin - metabolism; Cycle; Enzyme Activation; Fibroblasts - metabolism; Fibroblasts - pathology; Gene Expression Regulation, Neoplastic; Genetic Complementation Test; HeLa Cells; Histone-Lysine N-Methyltransferase - genetics; Histone-Lysine N-Methyltransferase - metabolism; Histones - genetics; Histones - metabolism; Humans; Landes; Life Sciences; Lysine - metabolism; Methylation; Mice; Mice, Inbred C57BL; Mice, Knockout; Mutagenesis, Site-Directed; Organogenesis; Peptide Library; Phenotype; Plasmids - genetics; Plasmids - metabolism; Proteins; Recombinant Proteins - genetics; Recombinant Proteins - metabolism; RNA, Small Interfering - genetics; RNA, Small Interfering - metabolism; Substrate Specificity
• ISSN: 1559-2294; 1559-2308
• DOI: 10.4161/epi.19506

Smyd3 is a lysine methyltransferase implicated in chromatin and cancer regulation. Here we show that Smyd3 catalyzes histone H4 methylation at lysine 5 (H4K5me). This novel histone methylation mark is detected in diverse cell types and its formation is attenuated by depletion of Smyd3 protein. Further, Smyd3-driven cancer cell phenotypes require its enzymatic activity. Thus, Smyd3, via H4K5 methylation, provides a potential new link between chromatin dynamics and neoplastic disease.