Molecular biology: Akt-mediated phosphorylation of EZH2 suppresses methylation of lysine 27 in histone H3

Tai Lung Cha; Binhua P. Zhou; Weiya Xia; Yadi Wu; Cheng Chieh Yang; Chun Te Chen; Bo Ping; Arie P. Otte; Mien Chie Hung

doi:10.1126/science.1118947

Molecular biology: Akt-mediated phosphorylation of EZH2 suppresses methylation of lysine 27 in histone H3

Tai Lung Cha, Binhua P. Zhou, Weiya Xia, Yadi Wu, Cheng Chieh Yang, Chun Te Chen, Bo Ping, Arie P. Otte, Mien Chie Hung

Research output: Contribution to journal › Article › peer-review

469 Scopus citations

Abstract

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.

Original language	English
Pages (from-to)	306-310
Number of pages	5
Journal	Science
Volume	310
Issue number	5746
DOIs	https://doi.org/10.1126/science.1118947
State	Published - Oct 14 2005

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title = "Molecular biology: Akt-mediated phosphorylation of EZH2 suppresses methylation of lysine 27 in histone H3",

abstract = "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.",

author = "Cha, {Tai Lung} and Zhou, {Binhua P.} and Weiya Xia and Yadi Wu and Yang, {Cheng Chieh} and Chen, {Chun Te} and Bo Ping and Otte, {Arie P.} and Hung, {Mien Chie}",

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T1 - Molecular biology

T2 - Akt-mediated phosphorylation of EZH2 suppresses methylation of lysine 27 in histone H3

AU - Cha, Tai Lung

AU - Zhou, Binhua P.

AU - Xia, Weiya

AU - Wu, Yadi

AU - Yang, Cheng Chieh

AU - Chen, Chun Te

AU - Ping, Bo

AU - Otte, Arie P.

AU - Hung, Mien Chie

PY - 2005/10/14

Y1 - 2005/10/14

N2 - 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.

AB - 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.

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Molecular biology: Akt-mediated phosphorylation of EZH2 suppresses methylation of lysine 27 in histone H3

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