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HDAC3 influences phosphorylation of STAT3 at serine 727 by interacting with PP2A

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Title: HDAC3 influences phosphorylation of STAT3 at serine 727 by interacting with PP2A
Other Titles: Interactions among STAT3, HDAC3 and PP2A
Authors: Togi, Sumihito Browse this author
Kamitani, Shinya Browse this author
Kawakami, Shiho Browse this author
Ikeda, Osamu Browse this author
Muromoto, Ryuta Browse this author
Nanbo, Asuka Browse this author
Matsuda, Tadashi Browse this author →KAKEN DB
Keywords: STAT3
PP2A
HDAC3
dephosphorylation
transcriptional regulation
Issue Date: 6-Feb-2009
Publisher: Academic Press
Journal Title: Biochemical and Biophysical Research Communications
Volume: 379
Issue: 2
Start Page: 616
End Page: 620
Publisher DOI: 10.1016/j.bbrc.2008.12.132
PMID: 19121623
Abstract: 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.
Type: article (author version)
URI: http://hdl.handle.net/2115/35328
Appears in Collections:薬学研究院 (Faculty of Pharmaceutical Sciences) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

Submitter: 松田 正

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