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

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Title: STAP-2 is phosphorylated at tyrosine-250 by Brk and modulates Brk-mediated STAT3 activation
Other Titles: Brk phosphorylates and regulates STAP-2 functions
Authors: Ikeda, Osamu Browse this author
Miyasaka, Yuto Browse this author
Sekine, Yuichi Browse this author
Mizushima, Akihiro Browse this author
Muromoto, Ryuta Browse this author
Nanbo, Asuka Browse this author
Yoshimura, Akihiko Browse this author
Matsuda, Tadashi Browse this author →KAKEN DB
Keywords: Brk
Issue Date: 19-Jun-2009
Publisher: Academic Press
Journal Title: Biochemical and Biophysical Research Communications
Volume: 384
Issue: 1
Start Page: 71
End Page: 75
Publisher DOI: 10.1016/j.bbrc.2009.04.076
PMID: 19393627
Abstract: 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.
Type: article (author version)
Appears in Collections:薬学研究院 (Faculty of Pharmaceutical Sciences) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

Submitter: 松田 正

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