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.
| Original language | English |
|---|---|
| Pages (from-to) | 517-522 |
| Number of pages | 6 |
| Journal | Biochemical and Biophysical Research Communications |
| Volume | 356 |
| Issue number | 2 |
| DOIs | |
| Publication status | Published - 2007 May 4 |
| Externally published | Yes |
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Keywords
- Adaptor protein
- Antibody
- LIF
- Phosphorylation
- STAP-2
- STAT3
- Transcription
ASJC Scopus subject areas
- Biochemistry
- Biophysics
- Molecular Biology
Cite this
Leukemia inhibitory factor-induced phosphorylation of STAP-2 on tyrosine-250 is involved in its STAT3-enhancing activity. / Sekine, Yuichi; Tsuji, Satoshi; Ikeda, Osamu; Kakisaka, Michinori; Sugiyama, Kenji; Yoshimura, Akihiko; Matsuda, Tadashi.
In: Biochemical and Biophysical Research Communications, Vol. 356, No. 2, 04.05.2007, p. 517-522.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Leukemia inhibitory factor-induced phosphorylation of STAP-2 on tyrosine-250 is involved in its STAT3-enhancing activity
AU - Sekine, Yuichi
AU - Tsuji, Satoshi
AU - Ikeda, Osamu
AU - Kakisaka, Michinori
AU - Sugiyama, Kenji
AU - Yoshimura, Akihiko
AU - Matsuda, Tadashi
PY - 2007/5/4
Y1 - 2007/5/4
N2 - 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.
AB - 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.
KW - Adaptor protein
KW - Antibody
KW - LIF
KW - Phosphorylation
KW - STAP-2
KW - STAT3
KW - Transcription
UR - http://www.scopus.com/inward/record.url?scp=33947355024&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=33947355024&partnerID=8YFLogxK
U2 - 10.1016/j.bbrc.2007.03.031
DO - 10.1016/j.bbrc.2007.03.031
M3 - Article
C2 - 17368569
AN - SCOPUS:33947355024
VL - 356
SP - 517
EP - 522
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
SN - 0006-291X
IS - 2
ER -