1.GlaxoSmithKline; Collegeville, PA USA;2.Department of Biolog; Stanford University; Stanford, CA USA;3.Department of Molecular Biology; Princeton University; Princeton NJ USA;4.Department of Pediatrics; Stanford School of Medicine; Stanford, CA USA;5.Department of Biology; Stanford University; Stanford, CA USA
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.