HDAC3 influences phosphorylation of STAT3 at serine 727 by interacting with PP2A
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概要
- 論文の詳細を見る
Signal transducer and activator of transcription 3 (STAT3), which mediates biological actions in many physiological processes, is activated by cytokines and growth factors, and has been reported to be involved in the pathogenesis of various human diseases. Here, we show that treatment of HeLa cells with a histone deacetylase (HDAC) inhibitor, trichostatin A, or small-interfering RNA (siRNA)-mediated repression of HDAC3, enhances phosphorylation of STAT3 at Ser727. Furthermore, dephosphorylation of STAT3 at Ser727 by protein phosphatase 2A (PP2A) was restored by treatment of cells with HDAC3 siRNA. We further found that formation of a complex between STAT3 and PP2A was enhanced in the presence of HDAC3. Importantly, smallinterfering RNA-mediated repression of both HDAC3 and PP2A effectively enhanced leukemia inhibitory factor (LIF)-induced STAT3 activation. These results indicate that HDAC3 may act as a scaffold protein for PP2A to regulate the LIF/STAT3-mediated signaling pathway.
- Academic Pressの論文
- 2009-02-06
著者
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Shimoda K
Department Of Internal Medicine Gastroenterology And Hematology Faculty Of Medicine Miyazaki Univers
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Shimoda Kazuya
九州大学 医学部病態情報学
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Shimoda Kazuya
九州大学 第1内科
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Muromoto Ryuta
Department Of Immunology Graduate School Of Pharmaceutical Sciences Hokkaido University
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Shimoda Kazuya
Medicine And Biosystemic Science Graduate School Of Medical Sciences Kyushu University
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Matsuda Tadashi
Department Of Immunology Graduate School Of Pharmaceutical Sciences Hokkaido University
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Sugiyama Kenji
Department Of Internal Medicine Gastroenterology And Hematology Faculty Of Medicine Miyazaki Univers
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Ikeda Osamu
Department Of Immunology Graduate School Of Pharmaceutical Sciences Hokkaido University
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Nanbo Asuka
Department Of Immunology Graduate School Of Pharmaceutical Sciences Hokkaido University
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