Project/Area Number |
14206009
|
Research Category |
Grant-in-Aid for Scientific Research (A)
|
Allocation Type | Single-year Grants |
Section | 一般 |
Research Field |
応用微生物学・応用生物化学
|
Research Institution | The University of Tokyo |
Principal Investigator |
FUKUI Yasuhisa The University of Tokyo, Graduate School of Agricultural and Life Sciences, Professor, 大学院・農学生命科学研究科, 教授 (00181248)
|
Co-Investigator(Kenkyū-buntansha) |
IHARA Sayoko The University of Tokyo, Graduate School of Agricultural and Life Sciences, Assistant, 大学院・農学生命科学研究科, 助手 (80292788)
|
Project Period (FY) |
2002 – 2004
|
Project Status |
Completed (Fiscal Year 2004)
|
Budget Amount *help |
¥51,480,000 (Direct Cost: ¥39,600,000、Indirect Cost: ¥11,880,000)
Fiscal Year 2004: ¥11,830,000 (Direct Cost: ¥9,100,000、Indirect Cost: ¥2,730,000)
Fiscal Year 2003: ¥11,700,000 (Direct Cost: ¥9,000,000、Indirect Cost: ¥2,700,000)
Fiscal Year 2002: ¥27,950,000 (Direct Cost: ¥21,500,000、Indirect Cost: ¥6,450,000)
|
Keywords | PI3 kinase / phosphatidylinositol / PIP_3 / plextrin / cell polarity / G protein / cell adhesion / cell motility / PI3キナーゼ |
Research Abstract |
Cell motility is often caused by cytoskeletal rearrangement. We found SWAP-70 as a protein which regulates actin rearrangement depending on phosphatidylinositol-3 kinase to be involved in membrane ruffling. SWAP-70 binds to activated Rac and F-actin. Kidney cells cultured from SWAP-70 deficient mice exhibits impaired membrane ruffling after EGF treatment. Def-6, a protein homologous to SWAP-70 lacks the F-actin binding site found in SWAP-70. This year, we explored the difference of these two proteins. The two proteins enhanced membrane ruffling when overexpressed in Cos7 cells, suggesting that these proteins are both involved in membrane ruffling. They both co-localized with activated Rac, however, the phenotypes were quite different. SWAP-70 induced membrane ruffling but Def-6 induced marked misshaping of the cells. The time lapse experiment revealed that this morphological change was reversible, suggesting that cells are quickly changing their shapes. These results suggest that the two proteins are highly homologous but they contributes to membrane ruffling in completely different ways. It is interesting to argue how the binding activity correlates with their functions.
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