Interactions of STAP-2 with Brk and STAT3 participate in cell growth  of human breast cancer cells.

Ikeda, Osamu; Sekine, Yuichi; Mizushima, Akihiko; Nakasuji, Misa; Miyasaka, Yuto; Yamamoto, Chikako; Muromoto, Ryuta; Nanbo, Asuka; Oritani, Kenji; Yoshimura, Akihiko; Matsuda, Tadashi

Interactions of STAP-2 with Brk and STAT3 participate in cell growth of human breast cancer cells.

Ikeda, Osamu; Sekine, Yuichi; Mizushima, Akihiko et al.

The Journal of Biological Chemistry, 2010, 285(49), 38093-38103

Permalink : https://hdl.handle.net/2115/44383

このアイテムのアクセス数:1,505件（2026-05-11 05:47 集計）

閲覧可能ファイル

ファイル	フォーマット	サイズ	閲覧回数	説明
JBC-revise	pdf	3.83 MB	1,272

論文情報

ファイル出力 EndNote Basic出力 Mendeley出力

アクセス権	open access
URI	https://hdl.handle.net/2115/44383
タイトル	Interactions of STAP-2 with Brk and STAT3 participate in cell growth of human breast cancer cells.
著者	Ikeda, Osamu ; Sekine, Yuichi ; Mizushima, Akihiko ; Nakasuji, Misa ; Miyasaka, Yuto ; Yamamoto, Chikako ; Muromoto, Ryuta ; Nanbo, Asuka ; Oritani, Kenji ; Yoshimura, Akihiko ; Matsuda, Tadashi
著者名 Ikeda, Osamu
著者名 Sekine, Yuichi
著者名 Mizushima, Akihiko
著者名 Nakasuji, Misa
著者名 Miyasaka, Yuto
著者名 Yamamoto, Chikako
e-Rad_Researcher 30455597 著者名 Muromoto, Ryuta
e-Rad_Researcher 60359487 著者名 Nanbo, Asuka
著者名 Oritani, Kenji
著者名 Yoshimura, Akihiko
著者名 Matsuda, Tadashi
言語	英語
キーワード	Adaptor proteins
	Breast cancer
	Protein phosphorylation
	Signal transduction
	Transcription factors
	Tyrosine protein kinase (Tyrosine kinase)
	Brk
	STAP-2
	STAT3
発行日	2010-12-06T05:39:50Z
収録物名	The Journal of Biological Chemistry
巻(号)	285(49)
ページ	38093-38103
抄録	Signal transducing adaptor protein-2 (STAP-2) is a recently identified adaptor protein, which contains pleckstrin homology (PH) and Src homology 2 (SH2)-like domains, as well as a signal transducer and an activator of transcription 3 (STAT3)-binding motif in its C-terminal region. STAP-2 is also a substrate of breast tumor kinase (Brk). In breast cancers, Brk expression is deregulated and it promotes STAT3-dependent cell proliferation. In the present study, manipulated STAP-2 expression demonstrated essential roles of STAP-2 in Brk-mediated STAT3 activation. STAP-2 interacts with both Brk and STAT3. In addition, small-interfering RNA-mediated reduction of endogenous STAP-2 expression strongly decreased Brk-mediated STAT3 activation in T47D breast cancer cells. The PH domain of STAP-2 is involved in multiple steps; the binding between Brk and STAP-2, the activation and tyrosine phosphorylation of STAT3, and the activation of Brk. Notably, a STAP-2 PH-Brk fusion protein exhibited robust kinase activity and increased activation and tyrosine phosphorylation of STAT3. Finally, STAP-2-knockdown in T47D cells induced a significant decrease of proliferation, as strong as that of Brk- or STAT3-knockdown. Taken together, our findings are likely to inform the development of a novel therapeutic strategy, as well as the determination of novel prognostic values, in breast carcinomas.
資源タイプ	学術雑誌論文
出版タイプ	Accepted Manuscript
権利情報	Copyright (c) [yyyy] the American Society for Biochemistry and Molecular Biology
PISSN	0021-9258
関連情報 (isVersionOf)	出版社版DOI https://doi.org/10.1074/jbc.M110.162388