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Study on signal transduction mechanism of p120 RasGAP piotein

Research Project

Project/Area Number 13672270
Research Category

Grant-in-Aid for Scientific Research (C)

Allocation TypeSingle-year Grants
Section一般
Research Field Biological pharmacy
Research InstitutionHOKKAIDO UNIVERSITY

Principal Investigator

MORIOKA Hiroshi  Hokkaido Univ., Grad.Sch.Pharm.Sci., Assoc.Prof., 大学院・薬学研究科, 助教授 (20230097)

Project Period (FY) 2001 – 2002
Project Status Completed (Fiscal Year 2002)
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)
KeywordsRasGAP / RhoGAP / Biacore / SH2 domain / SH3 domain / phosphorylated tyrosine / signal transduction / domain engineering / Ras / GTPase活性 / Proline Rich Region
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.

Report

(3 results)
  • 2002 Annual Research Report   Final Research Report Summary
  • 2001 Annual Research Report
  • Research Products

    (8 results)

All Other

All Publications (8 results)

  • [Publications] Kobayashi H.: "DNA binding mode of antibody fragments specific for TT photo-dimers."Phosphorus Sulfur and Silicon. 177. 1553-1556 (2002)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      2002 Final Research Report Summary
  • [Publications] Sakurai S.: "Preparation and crystallization of human flap endonuclease FEN-1 in complex with proliferating-cell nuclear antigen, PCNA."Acta Cryst.. D59. 933-935 (2003)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      2002 Final Research Report Summary
  • [Publications] Suzuki N.: "Syndecan binding sites in the laminin al chain G domain."Biochemistry. 42. 12625-12633 (2003)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      2002 Final Research Report Summary
  • [Publications] Kurosaki, Y.: "Pyrimidine dimer formation and oxidative damage in M13 bacteriophage inactivation by ultraviolet C irradiation."Photochem.Photobiol.. 78. 349-354 (2003)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      2002 Final Research Report Summary
  • [Publications] Kobayashi H., Komatsu Y., Morioka H., Ohtsuka E: "DNA binding mode of antibody fragments specific for TT photo-dimers."Phosphorus Sulfur and Silicon. 177. 1553-1556 (2002)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      2002 Final Research Report Summary
  • [Publications] Sakurai S., Kitano K., Okada K., Hamada K., Morioka H., Hakoshima T: "Preparation and crystallization of human flap endonuclease FEN-1 in complex with proliferating-cell nuclear antigen, PCNA."Acta Cryst.. D59. 933-935 (2003)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      2002 Final Research Report Summary
  • [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)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      2002 Final Research Report Summary
  • [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)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      2002 Final Research Report Summary

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Published: 2001-04-01   Modified: 2016-04-21  

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