Leukemia inhibitory factor-induced phosphorylation of STAP-2 on tyrosine-250 is involved in its STAT3-enhancing activity.

Sekine, Yuichi; Tsuji, Satoshi; Ikeda, Osamu; Kakisaka, Michinori; Sugiyama, Kenji; Yoshimura, Akihiko; Matsuda, Tadashi

Leukemia inhibitory factor-induced phosphorylation of STAP-2 on tyrosine-250 is involved in its STAT3-enhancing activity.

Sekine, Yuichi; Tsuji, Satoshi; Ikeda, Osamu et al.

Biochemical and Biophysical Research Communications, 2007, 356(2), 517-522

Permalink : https://hdl.handle.net/2115/22097

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アクセス権	open access
URI	https://hdl.handle.net/2115/22097
タイトル	Leukemia inhibitory factor-induced phosphorylation of STAP-2 on tyrosine-250 is involved in its STAT3-enhancing activity.
著者	Sekine, Yuichi ; Tsuji, Satoshi ; Ikeda, Osamu ; Kakisaka, Michinori ; Sugiyama, Kenji ; Yoshimura, Akihiko ; Matsuda, Tadashi
著者名 Sekine, Yuichi
著者名 Tsuji, Satoshi
著者名 Ikeda, Osamu
著者名 Kakisaka, Michinori
著者名 Sugiyama, Kenji
著者名 Yoshimura, Akihiko
e-Rad_Researcher 20212219 著者名 Matsuda, Tadashi
言語	英語
キーワード	STAP-2
	LIF
	Phosphorylation
	Adaptor protein
	STAT3
	Transcription
	Antibody
発行日	2007-05-04
出版者	Elsevier Inc.
収録物名	Biochemical and Biophysical Research Communications
巻(号)	356(2)
ページ	517-522
抄録	Signal transducing adaptor protein-2 (STAP-2) is a recently identified adaptor protein that contains Pleckstrin and Src homology 2 (SH2)-like domains as well as a YXXQ motif in its C-terminal region. Our previous studies revealed that STAP-2 binds to signal transducer and activator of transcription 3 (STAT3) and STAT5, and regulates their signaling pathways. In the present study, we identified tyrosine-250 (Tyr250) in STAP-2 as a major site of phosphorylation by v-src and Jak2, using a phospho-specific antibody against STAP-2 phosphorylated at Tyr250. Mutational analyses revealed that Tyr250 was involved in the STAT3-enhancing activity of STAP-2. We further found that leukemia inhibitory factor (LIF) stimulated STAP-2 Tyr250 phosphorylation in 293T and Hep3B cells. Moreover, endogenous STAP-2 was phosphorylated at Tyr250 following LIF stimulation of murine M1 cell line. Taken together, our findings demonstrate that endogenous STAP-2 is phosphorylated at Tyr250 and that this phosphorylation is involved in its function.
資源タイプ	学術雑誌論文
出版タイプ	Accepted Manuscript
PISSN	0006-291X
EISSN	1090-2104
関連情報	PMID 17368569
関連情報	URI http://www.sciencedirect.com/science/journal/0006291X
関連情報 (isVersionOf)	出版社版DOI https://doi.org/10.1016/j.bbrc.2007.03.031