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  G9a and Glp Methylate lysine 373 in the Tumor Suppressor p53

Huang, J., Dorsey, J., Schikov, S., Zhang, X., Jenuwein, T., Reinberg, D., et al. (2010). G9a and Glp Methylate lysine 373 in the Tumor Suppressor p53. Journal of Biological Chemistry, 285, 9636-9641.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002B-8E97-6 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002B-8E98-4
Genre: Journal Article

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 Creators:
Huang, Jing, Author
Dorsey, Jean, Author
Schikov, Sergei, Author
Zhang, Xinyue, Author
Jenuwein, Thomas1, Author              
Reinberg, Danny, Author
Berger, Shelley, Author
Affiliations:
1Department of Epigenetics, Max Planck Institute of Immunobiology and Epigenetics, Max Planck Society, ou_2243644              

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 Abstract: The tumor suppressor p53 is regulated by numerous post-translational modifications. Lysine methylation has recently emerged as a key post-translational modification that alters the activity of p53. Here, we describe a novel lysine methylation site in p53 that is carried out by two homologous histone methyltransferases, G9a and Glp. G9a and Glp specifically methylate p53 at Lys373, resulting mainly in dimethylation. During DNA damage, the overall level of p53 modified at Lys373me2 does not increase, despite the dramatic increase in total p53, indicating that Lys373me2 correlates with inactive p53. Further, reduction of G9a and/or Glp levels leads to a larger population of apoptotic cells. Examination of the Oncomine data base shows that G9a and Glp are overexpressed in various cancers compared with corresponding normal tissues, suggesting that they are putative oncogenes. These data reveal a new methylation site within p53 mediated by the methylases G9a and Glp and indicate that G9a is a potential inhibitory target for cancer treatment.

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Language(s): eng - English
 Dates: 2010-03-26
 Publication Status: Published in print
 Pages: -
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 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 529427
 Degree: -

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Title: Journal of Biological Chemistry
  Alternative Title : J. Biol. Chem.
Source Genre: Journal
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Pages: - Volume / Issue: 285 Sequence Number: - Start / End Page: 9636 - 9641 Identifier: -