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Leukemia inhibitory factor-induced phosphorylation of STAP-2 on tyrosine-250 is involved in its STAT3-enhancing activity.

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Title: Leukemia inhibitory factor-induced phosphorylation of STAP-2 on tyrosine-250 is involved in its STAT3-enhancing activity.
Authors: Sekine, Yuichi Browse this author
Tsuji, Satoshi Browse this author
Ikeda, Osamu Browse this author
Kakisaka, Michinori Browse this author
Sugiyama, Kenji Browse this author
Yoshimura, Akihiko Browse this author
Matsuda, Tadashi Browse this author →KAKEN DB
Keywords: STAP-2
Adaptor protein
Issue Date: 4-May-2007
Publisher: Elsevier Inc.
Journal Title: Biochemical and Biophysical Research Communications
Volume: 356
Issue: 2
Start Page: 517
End Page: 522
Publisher DOI: 10.1016/j.bbrc.2007.03.031
PMID: 17368569
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. Our previous studies revealed that STAP-2 binds to signal transducer and activator of transcription 3 (STAT3) and STAT5, and regulates their signaling pathways. In the present study, we identified tyrosine-250 (Tyr250) in STAP-2 as a major site of phosphorylation by v-src and Jak2, using a phospho-specific antibody against STAP-2 phosphorylated at Tyr250. Mutational analyses revealed that Tyr250 was involved in the STAT3-enhancing activity of STAP-2. We further found that leukemia inhibitory factor (LIF) stimulated STAP-2 Tyr250 phosphorylation in 293T and Hep3B cells. Moreover, endogenous STAP-2 was phosphorylated at Tyr250 following LIF stimulation of murine M1 cell line. Taken together, our findings demonstrate that endogenous STAP-2 is phosphorylated at Tyr250 and that this phosphorylation is involved in its function.
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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