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Epigenetics Volume 7, 2012 - Issue 4
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Brief Report

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

Glenn S. Van Aller GlaxoSmithKline; Collegeville, PA USACorrespondence[email protected]
,
Nicolas Reynoird Department of Biolog; Stanford University; Stanford, CA USA
,
Olena Barbash GlaxoSmithKline; Collegeville, PA USA
,
Michael Huddleston GlaxoSmithKline; Collegeville, PA USA
,
Shichong Liu Department of Molecular Biology; Princeton University; Princeton NJ USA
,
Anne-Flore Zmoos Department of Pediatrics; Stanford School of Medicine; Stanford, CA USA
,
Patrick McDevitt GlaxoSmithKline; Collegeville, PA USA
,
Robert Sinnamon GlaxoSmithKline; Collegeville, PA USA
,
BaoChau Le GlaxoSmithKline; Collegeville, PA USA
,
Gloria Mas Department of Biology; Stanford University; Stanford, CA USA
,
Roland Annan GlaxoSmithKline; Collegeville, PA USA
,
Julien Sage Department of Pediatrics; Stanford School of Medicine; Stanford, CA USA
,
Benjamin A. Garcia Department of Molecular Biology; Princeton University; Princeton NJ USA
,
Peter J. Tummino GlaxoSmithKline; Collegeville, PA USA
,
Or Gozani Department of Biology; Stanford University; Stanford, CA USACorrespondence[email protected]
&
Ryan G. Kruger GlaxoSmithKline; Collegeville, PA USACorrespondence[email protected]
 show all
Pages 340-343 | Received 14 Dec 2011, Accepted 27 Jan 2012, Published online: 01 Apr 2012
 
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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.

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