STAP-2 is phosphorylated at tyrosine-250 by Brk and modulates Brk-mediated STAT3 activation

Ikeda, Osamu; Miyasaka, Yuto; Sekine, Yuichi; Mizushima, Akihiro; Muromoto, Ryuta; Nanbo, Asuka; Yoshimura, Akihiko; Matsuda, Tadashi

STAP-2 is phosphorylated at tyrosine-250 by Brk and modulates Brk-mediated STAT3 activation

Ikeda, Osamu; Miyasaka, Yuto; Sekine, Yuichi et al.

Biochemical and Biophysical Research Communications, 2009, 384(1), 71-75

Permalink : https://hdl.handle.net/2115/38456

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アクセス権	open access
URI	https://hdl.handle.net/2115/38456
タイトル	STAP-2 is phosphorylated at tyrosine-250 by Brk and modulates Brk-mediated STAT3 activation
その他のタイトル	Brk phosphorylates and regulates STAP-2 functions
著者	Ikeda, Osamu ; Miyasaka, Yuto ; Sekine, Yuichi ; Mizushima, Akihiro ; Muromoto, Ryuta ; Nanbo, Asuka ; Yoshimura, Akihiko ; Matsuda, Tadashi
著者名 Ikeda, Osamu
著者名 Miyasaka, Yuto
著者名 Sekine, Yuichi
著者名 Mizushima, Akihiro
著者名 Muromoto, Ryuta
著者名 Nanbo, Asuka
著者名 Yoshimura, Akihiko
e-Rad_Researcher 20212219 著者名 Matsuda, Tadashi
言語	英語
キーワード	Brk
	STAP-2
	phosphorylation
	STAT3
	transcription
発行日	2009-06-19
出版者	Academic Press
収録物名	Biochemical and Biophysical Research Communications
巻(号)	384(1)
ページ	71-75
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. STAP-2 is also known as breast tumor kinase (Brk) substrate (BKS). Our previous studies revealed that STAP-2 binds to signal transducer and activator of transcription 3 (STAT3) and STAT5, and regulates the signaling pathways downstream of them. In the present study, we identified tyrosine-250 (Tyr250) in STAP-2 as a major site of phosphorylation by Brk, using a series of STAP-2 YF mutants and anti-phospho-STAP-2 Tyr250 antibody. Furthermore, overexpression of the STAP-2 Y250F mutant protein affected Brk-mediated STAT3 activation. Importantly, small-interfering RNA-mediated reduction of endogenous STAP-2 expression decreased Brk-mediated STAT3 activation. Taken together, our findings demonstrate that STAP-2 is phosphorylated at Tyr250 by Brk, and plays an important role in Brk-mediated STAT3 activation.
資源タイプ	学術雑誌論文
出版タイプ	Accepted Manuscript
PISSN	0006-291X
EISSN	1090-2104
NCID	AA00564395
関連情報	PMID 19393627
関連情報 (isVersionOf)	出版社版DOI https://doi.org/10.1016/j.bbrc.2009.04.076