A New STAT3-binding Partner, ARL3, Enhances the Phosphorylation and Nuclear Accumulation of STAT3

Togi, Sumihito; Muromoto, Ryuta; Hirashima, Koki; Kitai, Yuichi; Okayama, Taichiro; Ikeda, Osamu; Matsumoto, Naoki; Kon, Shigeyuki; Sekine, Yuichi; Oritani, Kenji; Matsuda, Tadashi

A New STAT3-binding Partner, ARL3, Enhances the Phosphorylation and Nuclear Accumulation of STAT3

Togi, Sumihito; Muromoto, Ryuta; Hirashima, Koki et al.

Journal of Biological Chemistry (JBC), 2016, 291(21), 11161-11171

Permalink : https://hdl.handle.net/2115/65506

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アクセス権	open access
URI	https://hdl.handle.net/2115/65506
タイトル	A New STAT3-binding Partner, ARL3, Enhances the Phosphorylation and Nuclear Accumulation of STAT3
著者	Togi, Sumihito ; Muromoto, Ryuta ; Hirashima, Koki ; Kitai, Yuichi ; Okayama, Taichiro ; Ikeda, Osamu ; Matsumoto, Naoki ; Kon, Shigeyuki ; Sekine, Yuichi ; Oritani, Kenji ; Matsuda, Tadashi
著者名 Togi, Sumihito
e-Rad_Researcher 30455597 著者名 Muromoto, Ryuta
著者名 Hirashima, Koki
e-Rad_Researcher 90756165 著者名 Kitai, Yuichi
著者名 Okayama, Taichiro
著者名 Ikeda, Osamu
著者名 Matsumoto, Naoki
e-Rad_Researcher 90344499 著者名 Kon, Shigeyuki
e-Rad_Researcher 20396295 著者名 Sekine, Yuichi
e-Rad_Researcher 70324762 著者名 Oritani, Kenji
e-Rad_Researcher 20212219 著者名 Matsuda, Tadashi
言語	英語
キーワード	gene transcription
	nuclear translocation
	protein phosphorylation
	signal transduction
	STAT3
発行日	2016-05-20
出版者	American Society for Biochemistry and Molecular Biology (ASBMB)
収録物名	Journal of Biological Chemistry (JBC)
巻(号)	291(21)
ページ	11161-11171
抄録	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.
資源タイプ	学術雑誌論文
出版タイプ	Version of Record
権利情報	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.
PISSN	0021-9258
関連情報 (isIdenticalTo)	出版社版DOI https://doi.org/10.1074/jbc.M116.724849