Phosphorylation of threonine-265 in Zipper-interacting protein kinase plays an important role in its activity and is induced by IL-6 family cytokines

Sato, Noriko; Kamada, Nobuyuki; Muromoto, Ryuta; Kawai, Taro; Sugiyama, Kenji; Watanabe, Tadashi; Imoto, Seiyu; Sekine, Yuichi; Ohbayashi, Norihiko; Ishida, Masato; Akira, Shizuo; Matsuda, Tadashi

Phosphorylation of threonine-265 in Zipper-interacting protein kinase plays an important role in its activity and is induced by IL-6 family cytokines

Sato, Noriko; Kamada, Nobuyuki; Muromoto, Ryuta et al.

Immunology Letters, 2006, 103(2), 127-134

Permalink : https://hdl.handle.net/2115/8407

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アクセス権	open access
URI	https://hdl.handle.net/2115/8407
タイトル	Phosphorylation of threonine-265 in Zipper-interacting protein kinase plays an important role in its activity and is induced by IL-6 family cytokines
著者	Sato, Noriko ; Kamada, Nobuyuki ; Muromoto, Ryuta ; Kawai, Taro ; Sugiyama, Kenji ; Watanabe, Tadashi ; Imoto, Seiyu ; Sekine, Yuichi ; Ohbayashi, Norihiko ; Ishida, Masato ; Akira, Shizuo ; Matsuda, Tadashi
著者名 Sato, Noriko
著者名 Kamada, Nobuyuki
著者名 Muromoto, Ryuta
著者名 Kawai, Taro
著者名 Sugiyama, Kenji
著者名 Watanabe, Tadashi
著者名 Imoto, Seiyu
著者名 Sekine, Yuichi
著者名 Ohbayashi, Norihiko
著者名 Ishida, Masato
著者名 Akira, Shizuo
e-Rad_Researcher 20212219 著者名 Matsuda, Tadashi
言語	英語
キーワード	ZIPK
	IL-6
	LIF
	apoptosis
	phosphorylation
発行日	2006-03-15
出版者	Elsevier
収録物名	Immunology Letters
巻(号)	103(2)
ページ	127-134
抄録	Zipper-interacting protein kinase (ZIPK) is a widely expressed serine/threonine kinase that has been implicated in cell death and transcriptional regulation, but its mechanism of regulation remains unknown. Here, we identified threonine-265 (Thr265) in ZIPK as a major autophosphorylation site. Mutational analyses revealed that autophosphorylation of Thr265 was essential for its full catalytic activity toward an exogenous substrate as well as for cell death induction. Furthermore, leukemia inhibitory factor (LIF) stimulated Thr265 phosphorylation of ZIPK, thereby leading to phosphorylation and activation of signal transducer and activator of transcription (STAT3). Taken together, our findings demonstrate that ZIPK is positively regulated through Thr265 phosphorylation and that this phosphorylation is essential for its function.
資源タイプ	学術雑誌論文
出版タイプ	Accepted Manuscript
PISSN	0165-2478
関連情報	PMID 16325270
関連情報	URI http://www.sciencedirect.com/science/journal/01652478
関連情報 (isVersionOf)	出版社版DOI https://doi.org/10.1016/j.imlet.2005.10.015