Involvement of STAP-2 in Brk-mediated phosphorylation and activation of STAT5 in breast cancer cells.

Ikeda, Osamu; Mizushima, Akihiro; Sekine, Yuichi; Yamamoto, Chikako; Muromoto, Ryuta; Nanbo, Asuka; Oritani, Kenji; Yoshimura, Akihiko; Matsuda, Tadashi

Involvement of STAP-2 in Brk-mediated phosphorylation and activation of STAT5 in breast cancer cells.

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

Cancer Science, 2011, 102(4), 756-761

Permalink : https://hdl.handle.net/2115/48965

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アクセス権	open access
URI	https://hdl.handle.net/2115/48965
タイトル	Involvement of STAP-2 in Brk-mediated phosphorylation and activation of STAT5 in breast cancer cells.
著者	Ikeda, Osamu ; Mizushima, Akihiro ; Sekine, Yuichi ; Yamamoto, Chikako ; Muromoto, Ryuta ; Nanbo, Asuka ; Oritani, Kenji ; Yoshimura, Akihiko ; Matsuda, Tadashi
著者名 Ikeda, Osamu
著者名 Mizushima, Akihiro
e-Rad_Researcher 20396295 著者名 Sekine, Yuichi
著者名 Yamamoto, Chikako
e-Rad_Researcher 30455597 著者名 Muromoto, Ryuta
e-Rad_Researcher 60359487 著者名 Nanbo, Asuka
e-Rad_Researcher 70324762 著者名 Oritani, Kenji
e-Rad_Researcher 90182815 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
	STAT5
	phosphorylation
	breast cancer
発行日	2011-04
出版者	Wiley
収録物名	Cancer Science
巻(号)	102(4)
ページ	756-761
抄録	Signal-transducing adaptor protein (STAP)-2 is a recently identified adaptor protein that contains Pleckstrin homology (PH) and Src homology 2 (SH2)-like domains, and is also known to be a substrate of breast tumor kinase (Brk). In a previous study, we found that STAP-2 upregulated Brk-mediated activation of signal transducer and activator of transcription (STAT) 3 in breast cancer cells. Here, we examined the involvement of STAP-2 in Brk-mediated STAT5 activation in breast cancer cells. Ectopic expression of STAP-2 induced Brk-mediated transcriptional activity of STAT5. Furthermore, STAP-2-knockdown in T47D breast cancer cells induced a marked decrease in proliferation that was as strong as that after Brk- or STAT5b-knockdown. Regarding the mechanism, the PH domain of STAP-2 is likely to participate in the process by which Brk phosphorylates and activates STAT5. Taken together, our findings provide insights toward the development of novel therapeutic strategies as well as 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	The definitive version is available at www.blackwell-synergy.com
PISSN	1347-9032
EISSN	1349-7006
NCID	AA11808050
関連情報	PMID 21205088
関連情報 (isVersionOf)	出版社版DOI https://doi.org/10.1111/j.1349-7006.2010.01842.x