Study on signal transduction mechanism of p120 RasGAP piotein
| Project/Area Number |
13672270
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Biological pharmacy
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| Research Institution | HOKKAIDO UNIVERSITY |
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Principal Investigator |
MORIOKA Hiroshi Hokkaido Univ., Grad.Sch.Pharm.Sci., Assoc.Prof., 大学院・薬学研究科, 助教授 (20230097)
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| Project Period (FY) |
2001 – 2002
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| Project Status |
Completed (Fiscal Year 2002)
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| Budget Amount *help |
¥3,600,000 (Direct Cost: ¥3,600,000)
Fiscal Year 2002: ¥1,300,000 (Direct Cost: ¥1,300,000)
Fiscal Year 2001: ¥2,300,000 (Direct Cost: ¥2,300,000)
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| Keywords | RasGAP / RhoGAP / Biacore / SH2 domain / SH3 domain / phosphorylated tyrosine / signal transduction / domain engineering / Ras / GTPase活性 / Proline Rich Region |
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| Research Abstract |
GTPase-activating proteins (GAPs) play an important role in signal tiansduction pathways regulated by small GTP-binding proteins RasGAP is composed of several domains. The C-terminus shows GAP activity as a negative regulator of Ras. The N-terminus contains SH2-SH3-SH2 that appears to be involved in interactions with signaling proteins, and functions as a Ras effector. These two SH2 domains have been found to associate stably with a tyrosine-phosphorylated protein, p190 RhoGAP, which is thought to regulate actin cytoskeleton dynamics. Several studies suggest that the interaction between Ras-GAP and Rho-GAP is regulated by phosphorylation of tyrosine residues, Tyr1087 and/or Tyr1105 in the middle domain of Rho-GAP, however, mechanisms for RasGAP-RhoGAP complex formation have not yet been determined.
To investigate these regulation mechanisms for molecular interactions, seven recombinant proteins composed of SH2(n)-SH3-SH2(c) domains of RasGAP have been prepared and subjected to binding assays against three kinds of tyrosine-phosphorylated synthetic peptides of p190 RhoGAP by means of biosensor (BIAcore) respectively. Results obtained from biosensor analysis revealed that both SH2(n) and SH2(c) domain could bind to each tyrosine-phosphorylated peptide. In addition, the protein containing both SH2(n) and SH2(c) domains synergistically bound to the dual tyrosine-phosphorylated peptide.
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Report
(3 results)
Research Products
(8 results)
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[Publications] Suzuki N., Ichikawa N., Kasai, S., Yamada M., Nishi N., Morioka H., Yamashita H., Kitagawa Y., Utani A., Hoffman M.P., Nomizu M: "Syndecan binding sites in the laminin al chain G domain."Biochemistry. 42. 12625-12633 (2003)
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[Publications] Kurosaki, Y., Abe, H., Morioka, H., Hirayama, J., Ikebuchi, K., Kamo, N., Nikaido, O., Azuma, H., Ikeda, H: "Pyrimidine dimer formation and oxidative damage in M13 bacteriophage inactivation by ultraviolet C irradiation."Photochem.Photobiol.. 78. 349-354 (2003)
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