2010 Fiscal Year Final Research Report
Analysis of the activation mechanism of FilGAP by phosphorylation in establishment and maintenance of cell polarity.
Project/Area Number |
21870031
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Research Category |
Grant-in-Aid for Research Activity Start-up
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Allocation Type | Single-year Grants |
Research Field |
Functional biochemistry
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Research Institution | Kitasato University |
Principal Investigator |
NAKAZAWA Yuki Kitasato University, 理学部, 助教 (50508851)
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Project Period (FY) |
2009 – 2010
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Keywords | 細胞極性 / リン酸化 |
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.
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Research Products
(1 results)