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Analysis of the activation mechanism of FilGAP by phosphorylation in establishment and maintenance of cell polarity.

Research Project

Project/Area Number 21870031
Research Category

Grant-in-Aid for Research Activity Start-up

Allocation TypeSingle-year Grants
Research Field Functional biochemistry
Research InstitutionKitasato University

Principal Investigator

NAKAZAWA Yuki  Kitasato University, 理学部, 助教 (50508851)

Project Period (FY) 2009 – 2010
Project Status Completed (Fiscal Year 2010)
Budget Amount *help
¥2,756,000 (Direct Cost: ¥2,120,000、Indirect Cost: ¥636,000)
Fiscal Year 2010: ¥1,313,000 (Direct Cost: ¥1,010,000、Indirect Cost: ¥303,000)
Fiscal Year 2009: ¥1,443,000 (Direct Cost: ¥1,110,000、Indirect Cost: ¥333,000)
Keywords細胞極性 / リン酸化 / シグナル伝達
Research Abstract

To understand the activation mechanism of the Rac GAP FilGAP, several FilGAP-binding proteins were isolated and identified by mass-spectrometry. Theanalysis demonstrated that FilGAP forms complexes with several RNA binding proteins. Oneof them, RBM10 was found to bind to FilGAP at cell edges and its tyrosine phosphorylationby Src-family enhances their binding. It appeared that RBM10 regulates expression ofFilGAP. In addition, analysis using an antibody against phosphorylated(activated) FilGAPdemonstrated the activation level of FilGAP during cell spreading.

Report

(3 results)
  • 2010 Annual Research Report   Final Research Report ( PDF )
  • 2009 Annual Research Report
  • Research Products

    (1 results)

All 2009

All Presentation (1 results)

  • [Presentation] RacGAP因子FilGAPのリン酸化による制御機構について2009

    • Author(s)
      中澤友紀、太田安隆
    • Organizer
      生体運動合同班会議
    • Place of Presentation
      東京
    • Related Report
      2010 Final Research Report

URL: 

Published: 2009-04-01   Modified: 2016-04-21  

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