| Project/Area Number |
07558091
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| Research Category |
Grant-in-Aid for Scientific Research (A)
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| Allocation Type | Single-year Grants |
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| Section | 展開研究 |
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| Research Field |
Structural biochemistry
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| Research Institution | The University of Tokyo |
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Principal Investigator |
TAKENAWA Tadaomi The University of Tokyo The Institute of Medical Science, Professor, 医科学研究所, 教授 (40101315)
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| Co-Investigator(Kenkyū-buntansha) |
FUKAMI Kiyoko The University of Tokyo The Institute of Medical Science, Research Associate, 医科学研究所, 助手 (40181242)
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| Project Period (FY) |
1995 – 1997
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| Project Status |
Completed (Fiscal Year 1997)
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| Budget Amount *help |
¥13,000,000 (Direct Cost: ¥13,000,000)
Fiscal Year 1997: ¥2,600,000 (Direct Cost: ¥2,600,000)
Fiscal Year 1996: ¥2,800,000 (Direct Cost: ¥2,800,000)
Fiscal Year 1995: ¥7,600,000 (Direct Cost: ¥7,600,000)
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| Keywords | N-WASP / Ash / Grb2 / filopodia / actin / tyrosine kinase / Grb2 / SH2ドメイン / SH3ドメイン / ホスホリパーゼCγ1 / SH_2ドメイン / SH_3ドメイン / ホスホリパーゼC_γ1 |
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| Research Abstract |
We found an adaptor protein, Ash/Grb2 which transmits tyrosine kinase signals to downstream, resulting in activation of Ras. This protein has one SH2 and two SH3 domains. In this project, we attempted to clarify binding proteins to Ash/Grb2 SH3 domain, and then purified SH3-binding proteins from bovine brain. Among them, two proteins (150 kDa and 65 kDa proteins) were new. After cDNA clonings of these proteins, 150 kDa protein was found to be one of synaptojamin isozymes. On the other hand, 65 kDa protein was found to be homologous to Wiskott-Aldrich syndrome protein (WASP). We therefore named it N-WASP.N-WASP has a PH domain, GBD/CRIB motif, IQ motif, verprolin-like motif, cofilin-like motif and proline-rich sequences. It binds to Ash/Grb2 SH3 domain and is activated downstream of tyrosine kinases. Activated N-WASP polymerizes actin filament in Cdc42 dependent manner, resulting in filopodia formation.
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