title: Smyd3 regulates cancer cell phenotypes and catalyzes histone H4 lysine 5 methylation.
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.
authors.affiliation: GlaxoSmithKline, Collegeville, PA, USA.
authors.forename: Glenn S
authors.initials: GS
authors.lastname: Van Aller
authors.forename: Nicolas
authors.initials: N
authors.lastname: Reynoird
authors.forename: Olena
authors.initials: O
authors.lastname: Barbash
authors.forename: Michael
authors.initials: M
authors.lastname: Huddleston
authors.forename: Shichong
authors.initials: S
authors.lastname: Liu
authors.forename: Anne-Flore
authors.initials: AF
authors.lastname: Zmoos
authors.forename: Patrick
authors.initials: P
authors.lastname: McDevitt
authors.forename: Robert
authors.initials: R
authors.lastname: Sinnamon
authors.forename: BaoChau
authors.initials: B
authors.lastname: Le
authors.forename: Gloria
authors.initials: G
authors.lastname: Mas
authors.forename: Roland
authors.initials: R
authors.lastname: Annan
authors.forename: Julien
authors.initials: J
authors.lastname: Sage
authors.forename: Benjamin A
authors.initials: BA
authors.lastname: Garcia
authors.forename: Peter J
authors.initials: PJ
authors.lastname: Tummino
authors.forename: Or
authors.initials: O
authors.lastname: Gozani
authors.forename: Ryan G
authors.initials: RG
authors.lastname: Kruger
mesh_terms: D000818:Animals; D015153:Blotting, Western; D002843:Chromatin / Q000235:genetics / Q000378:metabolism; D004789:Enzyme Activation; D005347:Fibroblasts / Q000378:metabolism / Q000473:pathology; D015972:Gene Expression Regulation, Neoplastic; D005816:Genetic Complementation Test; D006367:HeLa Cells; D011495:Histone-Lysine N-Methyltransferase / Q000235:genetics / Q000378:metabolism*; D006657:Histones / Q000235:genetics / Q000378:metabolism*; D006801:Humans; D008239:Lysine / Q000378:metabolism*; D008745:Methylation; D051379:Mice; D008810:Mice, Inbred C57BL; D018345:Mice, Knockout; D016297:Mutagenesis, Site-Directed; D019151:Peptide Library; D010641:Phenotype; D010957:Plasmids / Q000235:genetics / Q000378:metabolism; D034741:RNA, Small Interfering / Q000235:genetics / Q000378:metabolism; D011994:Recombinant Proteins / Q000235:genetics / Q000378:metabolism; D013379:Substrate Specificity
chemical_list: D002843:Chromatin; D006657:Histones; D019151:Peptide Library; D034741:RNA, Small Interfering; D011994:Recombinant Proteins; D011495:Histone-Lysine N-Methyltransferase; C506278:SMYD3 protein, human; D008239:Lysine