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.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
MeSH terms
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Animals
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Blotting, Western
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Chromatin / genetics
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Chromatin / metabolism
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Enzyme Activation
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Fibroblasts / metabolism
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Fibroblasts / pathology
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Gene Expression Regulation, Neoplastic*
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Genetic Complementation Test
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HeLa Cells
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Histone-Lysine N-Methyltransferase / genetics
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Histone-Lysine N-Methyltransferase / metabolism*
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Histones / genetics
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Histones / metabolism*
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Humans
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Lysine / metabolism*
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Methylation
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Mice
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Mice, Inbred C57BL
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Mice, Knockout
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Mutagenesis, Site-Directed
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Peptide Library
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Phenotype
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Plasmids / genetics
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Plasmids / metabolism
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RNA, Small Interfering / genetics
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RNA, Small Interfering / metabolism
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Recombinant Proteins / genetics
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Recombinant Proteins / metabolism
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Substrate Specificity
Substances
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Chromatin
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Histones
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Peptide Library
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RNA, Small Interfering
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Recombinant Proteins
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Histone-Lysine N-Methyltransferase
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SMYD3 protein, human
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Lysine