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A New STAT3-binding Partner, ARL3, Enhances the Phosphorylation and Nuclear Accumulation of STAT3
Title: | A New STAT3-binding Partner, ARL3, Enhances the Phosphorylation and Nuclear Accumulation of STAT3 |
Authors: | Togi, Sumihito Browse this author | Muromoto, Ryuta Browse this author →KAKEN DB | Hirashima, Koki Browse this author | Kitai, Yuichi Browse this author →KAKEN DB | Okayama, Taichiro Browse this author | Ikeda, Osamu Browse this author | Matsumoto, Naoki Browse this author | Kon, Shigeyuki Browse this author →KAKEN DB | Sekine, Yuichi Browse this author →KAKEN DB | Oritani, Kenji Browse this author →KAKEN DB | Matsuda, Tadashi Browse this author →KAKEN DB |
Keywords: | gene transcription | nuclear translocation | protein phosphorylation | signal transduction | STAT3 |
Issue Date: | 20-May-2016 |
Publisher: | American Society for Biochemistry and Molecular Biology (ASBMB) |
Journal Title: | Journal of Biological Chemistry (JBC) |
Volume: | 291 |
Issue: | 21 |
Start Page: | 11161 |
End Page: | 11171 |
Publisher DOI: | 10.1074/jbc.M116.724849 |
Abstract: | Signal transducer and activator of transcription 3 (STAT3) is involved in cell proliferation, differentiation, and cell survival during immune responses, hematopoiesis, neurogenesis, and other biological processes. STAT3 activity is regulated by a variety of mechanisms, including phosphorylation and nuclear translocation. To clarify the molecular mechanisms underlying the regulation of STAT3 activity, we performed yeast two-hybrid screening. We identified ARL3 (ADP-ribosylation factor-like 3) as a novel STAT3-binding partner. ARL3 recognizes the DNA-binding domain as well as the C-terminal region of STAT3 in vivo, and their binding was the strongest when both proteins were activated. Importantly, small interfering RNA-mediated reduction of endogenous ARL3 expression decreased IL-6-induced tyrosine phosphorylation, nuclear accumulation, and transcriptional activity of STAT3. These results indicate that ARL3 interacts with STAT3 and regulates the transcriptional activation of STAT3 by influencing its nuclear accumulation of STAT3. |
Rights: | This research was originally published in Journal of Biological Chemistry. Sumihito Togi, Ryuta Muromoto, Koki Hirashima, Yuichi Kitai, Taichiro Okayama, Osamu Ikeda, Naoki Matsumoto, Shigeyuki Kon, Yuichi Sekine, Kenji Oritani and Tadashi Matsuda. A New STAT3-binding Partner, ARL3, Enhances the Phosphorylation and Nuclear Accumulation of STAT3. Journal of Biological Chemistry. 2016; Vol.291:11161-11171. ©the American Society for Biochemistry and Molecular Biology. |
Type: | article |
URI: | http://hdl.handle.net/2115/65506 |
Appears in Collections: | 薬学研究院 (Faculty of Pharmaceutical Sciences) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)
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Submitter: 松田 正
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