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  • Articles  (1)
  • Latest Papers from Table of Contents or Articles in Press  (1)
  • HeLa Cells  (1)
  • Acetylation
  • Genomic Imprinting
  • Polycomb Repressive Complex 2
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    Akt-mediated phosphorylation of EZH2 suppresses methylation of lysine 27 in histone H3 (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-10-15
    Description: Enhancer of Zeste homolog 2 (EZH2) is a methyltransferase that plays an important role in many biological processes through its ability to trimethylate lysine 27 in histone H3. Here, we show that Akt phosphorylates EZH2 at serine 21 and suppresses its methyltransferase activity by impeding EZH2 binding to histone H3, which results in a decrease of lysine 27 trimethylation and derepression of silenced genes. Our results imply that Akt regulates the methylation activity, through phosphorylation of EZH2, which may contribute to oncogenesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cha, Tai-Lung -- Zhou, Binhua P -- Xia, Weiya -- Wu, Yadi -- Yang, Cheng-Chieh -- Chen, Chun-Te -- Ping, Bo -- Otte, Arie P -- Hung, Mien-Chie -- P01 099031/PHS HHS/ -- R01 109311/PHS HHS/ -- New York, N.Y. -- Science. 2005 Oct 14;310(5746):306-10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cellular Oncology, the University of Texas M. D. Anderson Cancer Center, Houston, TX 77030, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16224021" target="_blank"〉PubMed〈/a〉
    Keywords: 3T3 Cells ; Animals ; COS Cells ; Cell Line ; Cell Transformation, Neoplastic ; Cercopithecus aethiops ; Chromones/pharmacology ; DNA-Binding Proteins ; Enzyme Inhibitors/pharmacology ; Gene Expression Regulation ; HeLa Cells ; Histone-Lysine N-Methyltransferase/metabolism ; Histones/*metabolism ; Homeodomain Proteins/genetics ; Humans ; Lysine/*metabolism ; Methylation ; Mice ; Molecular Sequence Data ; Morpholines/pharmacology ; Phosphorylation ; Polycomb Repressive Complex 2 ; Protein Binding ; Protein Methyltransferases ; Protein-Serine-Threonine Kinases/antagonists & inhibitors/*metabolism ; Proteins/*metabolism ; Proto-Oncogene Proteins/antagonists & inhibitors/*metabolism ; Proto-Oncogene Proteins c-akt ; Serine/metabolism ; Transcription Factors
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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