| Project/Area Number |
25460067
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Multi-year Fund |
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| Section | 一般 |
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| Research Field |
Biological pharmacy
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| Research Institution | Nagasaki University |
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Principal Investigator |
TANIMURA Susumu 長崎大学, 医歯薬学総合研究科(薬学系), 助教 (90343342)
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| Co-Investigator(Kenkyū-buntansha) |
TAKEDA Kohsuke 長崎大学, 医歯薬学総合研究科(薬学系), 教授 (10313230)
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| Research Collaborator |
ARICHIKA Naoya
HAMAMATSU Ayako
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| Project Period (FY) |
2013-04-01 – 2016-03-31
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| Project Status |
Completed (Fiscal Year 2015)
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| Budget Amount *help |
¥5,200,000 (Direct Cost: ¥4,000,000、Indirect Cost: ¥1,200,000)
Fiscal Year 2015: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2014: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2013: ¥2,080,000 (Direct Cost: ¥1,600,000、Indirect Cost: ¥480,000)
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| Keywords | ミオシン / カベオラ / リン酸化 / 細胞運動 / 癌 / Caveolae / Myosin |
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| Outline of Final Research Achievements |
We have shown that SH3P2, a negative regulator of cell migration, interacts with Myosin1E (Myo1E) and prevents the localization of Myo1E to the lamellipodial tips. Dissociation of Myo1E from SH3P2 results in the induction of cell motility; however, the molecular mechanism of which still remains unknown. Here, we show that the SH3 domain of Myo1E bound to the Cavin1/3-Caveolin1 complex via the proline-rich region of Cavin3. RNAi-mediated depletion of Myo1E or Cavin3 suppressed the internalization of the Cavin1/3-Caveolin1 complex, the localized activation of Akt, and cell motility. We also revealed that Hsp90 co-chaperone proteins, UNC45 and STIP1, also interact with Myo1E and regulate the localization and expression level of Myo1E, respectively. These results suggest that the function of Myo1E is regulated by SH3P2, UNC45 and STIP1 and that Myo1E induces the localized activation of Akt through the Caveolae regulation and thus cell motility.
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