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Nuclear retention of STAT3 through the coiled-coil domain regulates its activity.

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タイトル: Nuclear retention of STAT3 through the coiled-coil domain regulates its activity.
著者: Sato, Noriko 著作を一覧する
Tsuruma, Rieko 著作を一覧する
Imoto, Seiyu 著作を一覧する
Sekine, Yuichi 著作を一覧する
Muromoto, Ryuta 著作を一覧する
Sugiyama, Kenji 著作を一覧する
Matsuda, Tadashi 著作を一覧する
キーワード: IL-6
Nuclear translocation
発行日: 2005年10月21日
出版者: Elsevier Inc.
誌名: Biochemical and Biophysical Research Communications
巻: 336
号: 2
開始ページ: 617
終了ページ: 624
出版社 DOI: 10.1016/j.bbrc.2005.08.145
抄録: Signal transducer and activator of transcription 3 (STAT3), which mediates biological actions in many physiological processes, is activated by cytokines and growth factors via specific tyrosine phosphorylation, dimerization, and nuclear translocation. However, the mechanism involved in its nuclear translocation remains unclear. A previous study demonstrated that STAT3 with Arg-214/215 mutations in the coiled-coil domain (R214A/R215A; STAT3 RA) failed to undergo nuclear translocation. Here, we re-examined the nature of the STAT3 RA mutant and found that it showed higher and more extensive tyrosine-phosphorylation as well as much higher STAT3 transcriptional activity in response to stimuli. Furthermore, STAT3 RA showed nuclear translocation and faster nuclear export than wild-type STAT3 after stimulation. Moreover, nuclear retention of STAT3 RA by a chromosomal region maintenance 1 (CRM1) inhibitor, leptomycin B, decreased the enhanced STAT3 activation by stimuli. These data demonstrate that Arg-214/215 are involved in CRM1-mediated STAT3 nuclear export and the regulation of STAT3 activity.
Relation (URI):
資料タイプ: article (author version)
出現コレクション:雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

提供者: 松田 正


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