Work

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

Year: 2012

Type: article

Abstract: 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.

Source: Epigenetics

DOI: 10.4161/epi.19506

Authors: Glenn S. Van Aller, Nicolas Reynoird, Olena Barbash, Michael Huddleston, Shichong Liu, Anne-Flore Zmoos, Patrick McDevitt, Robert Sinnamon, BaoChau Le, Gloria Mas, Roland Annan, Julien Sage, Benjamin A. Garcia, Peter J. Tummino, Or Gozani, Ryan G. Kruger

Institutions: GlaxoSmithKline (United Kingdom), GlaxoSmithKline (United States), Stanford University, Princeton University, Stanford Medicine

Language: English

Topic: Cancer-related gene regulation

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

SDG: Good health and well-being

Open Access status: hybrid

Funders: National Institutes of Health, National Institute of General Medical Sciences

Awards: Function of PHD Domain Proteins in Chromatin Regulation, G9000184591

OpenAlex ID: W2051406272

FWCI: 5.109

Cites: 10

Cited by: 170

Related to: 10