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Funtional analysis of Rhes, a novel Ras family protein, in neuronal cell

Research Project

Project/Area Number 14570125
Research Category

Grant-in-Aid for Scientific Research (C)

Allocation TypeSingle-year Grants
Section一般
Research Field Pathological medical chemistry
Research InstitutionUniversity of the Ryukyus

Principal Investigator

KARIYA Ken-ichi  University of the Ryukyus, Graduate School of Medicine, Professor, 大学院・医学研究科, 教授 (40263371)

Co-Investigator(Kenkyū-buntansha) UMIKAWA Masato  University of the Ryukyus, Graduate School of Medicine, Associate Professor, 大学院・医学研究科, 助教授 (00325838)
Project Period (FY) 2002 – 2003
Project Status Completed (Fiscal Year 2003)
Budget Amount *help
¥3,100,000 (Direct Cost: ¥3,100,000)
Fiscal Year 2003: ¥1,300,000 (Direct Cost: ¥1,300,000)
Fiscal Year 2002: ¥1,800,000 (Direct Cost: ¥1,800,000)
KeywordsRhes / Ras / MAP4K / Rap2 / Neuron / Rasファミリー / 神経細胞 / 低分子量GTP結合蛋白質 / シグナル伝達
Research Abstract

Rhes is a member of the Ras family small GTP-binding proteins. Rhes is expressed abundantly in brain, especially in striatum, and thus designated Ras homologue enriched in striatum. In the present study, we aimed at identifying a downstream effector molecule of Rhes thereby gaining insights into Rhes's neuronal function. Rhes's effector-binding domain is different from those of typical Ras homologue, suggesting interaction of Rhes with non-typical Ras effectors. Only one member of Ras family, Rap2, shares similar effector-binding region with Rhes. Rap2 shares Phe residue at the 8th position of effector-binding domain with Rhes, where Ras has Ser. Rap2 is expressed in brain and implicated in neuronal functions as well. We therefore reasoned that Rhes and Rap2 could share common non-typical Ras effectors. We used the yeast two-hybrid screening and affinity purification-mass spectrometry approach to search for Rlies-or Rap2-binding proteins. Unexpectedly, we isolated different binding proteins for Rhes and Rap2, such as ARMS(for Rhes) and MAP4K4(for Rap2). ARMS is a downstream molecule of NGF receptor, while MAP4K4's Drosophila homologue regulates neuronal axon targeting. Further studies are necessary to clarify physiological significances of these findings.

Report

(3 results)
  • 2003 Annual Research Report   Final Research Report Summary
  • 2002 Annual Research Report
  • Research Products

    (4 results)

All Other

All Publications (4 results)

  • [Publications] Machida, N., et al.: "Mitogen-activated protein kinase kinase kinase kinase 4 as a putative effector of Rap2 to activate the c-Jun N-terminal kinase."J.Biol.Chem.. (in press). (2004)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      2003 Final Research Report Summary
  • [Publications] Machida, N., Umikawa, M., Takei, K., Sakima, N., Myagmar, B.E., Taira, K., Uezato, H., Ogawa, Y., Kariya, K.: "Mitogen-activated protein kinase kinase kinase kinase 4 as a putative effector of Rap2 to activate the c-Jun N-terminal kinase."J.Biol.Chem.. (in press). (2004)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      2003 Final Research Report Summary
  • [Publications] Machida, N., et al.: "Mitogen-activated protein kinase kinase kinase kinase 4 as a putative effector of Rap2 to activate the c-Jun N-terminal kinase"J.Biol.Chem.. (in press). (2004)

    • Related Report
      2003 Annual Research Report
  • [Publications] Kido, M., et al.: "Critical function of the Ras-associating domain as a primary Ras-binding site for regulation of Saccharomyces cerevisiae adenylyl cyclase"J.Biol.Chem.. 277・5. 3117-3123 (2002)

    • Related Report
      2002 Annual Research Report

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Published: 2002-04-01   Modified: 2016-04-21  

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