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Analysis of a novel signaling system, the Rap2-MAP4K signaling complex

Research Project

Project/Area Number 18590303
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, Division of Cell Biology, Professr (40263371)

Project Period (FY) 2006 – 2007
Project Status Completed (Fiscal Year 2007)
Budget Amount *help
¥3,550,000 (Direct Cost: ¥3,100,000、Indirect Cost: ¥450,000)
Fiscal Year 2007: ¥1,950,000 (Direct Cost: ¥1,500,000、Indirect Cost: ¥450,000)
Fiscal Year 2006: ¥1,600,000 (Direct Cost: ¥1,600,000)
Keywordssignal transduction / Rap2 / MAP4K / MAPKKKキナーゼ / シグナル複合体 / NIK / HGK / TNIK / MINK
Research Abstract

We have previously shown that a Ras family small GTP-binding protein Rap2 interacts specifically with MAPKKK kinases (MAP4Ks) that activate the stress-activated MAPK, c-Jun N-terminal kinase (JNK). We believe that Rap2 and MAP4Ks interact with upstream molecules for regulation of Rap2 in response to upstream signals and downstream molecules for transmission of MAP4K signals and that they form a signaling complex, termed Rap2-MAP4K signaling complex. In the present study, we have examined the regulatory mechanisms and cellular functions of this complex, using an epidermal cell line as a model.
1. Components and regulatory mechanisms of the signaling complex
In order to identify major components of the signaling complex, we searched for molecules that interact with MAP4Ks. We have identified a protein of approximately 200 kDa (p200) containing the central repeat structure, cystein-rich domain and a C-terminal PDZ-binding motif. This protein appeared to be a mammalian homolog of a Drosophila scaffold protein. We also believe that the complex contains a dimer or oligomer of MAP4Ks.
2. Functional analysis of the signaling complex
In fibroblastic cells, Rap2-MAP4K complex regulates cell-substratum adhesion. On the other hand, in epithelial cells, the complex appeared to regulate cell-cell adhesion. We have used a retrovirus system to establish cell lines in that expression of tagged MAP4Ks can be regulated by tetracycline (Tet-Off). Over-expression of MAP4Ks, but not kinase-deficient mutants, negatively regulated cell-cell adhesion.

Report

(3 results)
  • 2007 Annual Research Report   Final Research Report Summary
  • 2006 Annual Research Report
  • Research Products

    (3 results)

All 2007

All Presentation (3 results)

  • [Presentation] TNIK (Traf2- and Nck-interacting kinase)結合蛋白質の同定と機能解析2007

    • Author(s)
      國仲弘一, 他
    • Organizer
      BMB2007(第30回日本分子生物学会年会・第80回日本生化学会大会合同大会)
    • Place of Presentation
      パシフィコ横浜
    • Year and Date
      2007-12-11
    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      2007 Final Research Report Summary
  • [Presentation] Identification and characterization of TNIK interacting Protein.2007

    • Author(s)
      Kuninaka K, Oshiro M, Umikawa M, Bayarjargal M, Yamashiro Y, Suzuki T, Kariya K.
    • Organizer
      Biochemistry and Molecular Biology 2007
    • Place of Presentation
      Pacifico Yokohama, Japan
    • Year and Date
      2007-12-11
    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      2007 Final Research Report Summary
  • [Presentation] TNIK(Traf2-and Nck-interacting kinase)結合蛋白質の同定と機能解析2007

    • Author(s)
      國仲弘一, 他
    • Organizer
      BMB2007(第30回日本分子生物学会年会・第80回日本生化学会大会 合同大会)
    • Place of Presentation
      パシフィコ横浜
    • Year and Date
      2007-12-11
    • Related Report
      2007 Annual Research Report

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Published: 2006-04-01   Modified: 2016-04-21  

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