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Physical and functional interactions between STAP-2/BKS and STAT5.

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Please use this identifier to cite or link to this item:http://hdl.handle.net/2115/28113

Title: Physical and functional interactions between STAP-2/BKS and STAT5.
Authors: Sekine, Yuichi Browse this author
Yamamoto, Tetsuya Browse this author
Yumioka, Taro Browse this author
Sugiyama, Kenji Browse this author
Tsuji, Satoshi Browse this author
Oritani, Kenji Browse this author
Shimoda, Kazuya Browse this author
Minoguchi, Mayu Browse this author
Yoshimura, Akihiko Browse this author
Matsuda, Tadashi Browse this author →KAKEN DB
Issue Date: 4-Mar-2005
Publisher: American Society for Biochemistry and Molecular Biology
Journal Title: Journal of Biological Chemistry
Volume: 280
Issue: 9
Start Page: 8188
End Page: 8196
Publisher DOI: 10.1074/jbc.M411692200
PMID: 15611091
Abstract: Signal-transducing adaptor protein family of proteins (STAPs), which currently contains two members, are proposed to be adaptor molecules because of their pleckstrin homology (PH) and Src-homology 2 (SH2)-like domains. STAP-1 has been shown to interact with STAT5 and the tyrosine kinase Tec. With regard to STAP-2/BKS functions, immunoprecipitation experiments and intracellular stainings revealed STAP-2/BKS binds STAT5 in several types of cells. Mutational studies revealed that the PH- and SH2-like domains of STAP-2/BKS interacted with the C-terminal region of STAT5. STAP-2/BKS and STAT5 were found to constitutively co-localize in the cytoplasm of resting cells, but STAP-2/BKS was found to dissociate upon STAT5 phosphorylation, suggesting a role in regulating signaling of STAT5. The physiological role of these interactions is not fully understood, but in studies of overexpression of STAP-2/BKS, cytokine-induced tyrosine phosphorylation and transcriptional activation of STAT5 was diminished. In addition, thymocytes from STAP-2/BKS-deficient mice showed the enhanced interleukin-2-dependent cell growth. Taken together, STAP-2/BKS is an additional modulator of STAT5-mediated signaling.
Rights: Copyright © 2005 by the American Society for Biochemistry and Molecular Biology
Type: article (author version)
URI: http://hdl.handle.net/2115/28113
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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