| Project/Area Number |
25410187
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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 |
Bio-related chemistry
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| Research Institution | Suntory Foundation for Life Sciences |
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Principal Investigator |
Miura Kaoru 公益財団法人サントリー生命科学財団, その他部局等, 研究員 (90353515)
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| Co-Investigator(Renkei-kenkyūsha) |
SHIMANOTO Keiko 公益財団法人サントリー生命科学財団, 生物有機科学研究所, 研究員 (70235638)
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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: ¥1,170,000 (Direct Cost: ¥900,000、Indirect Cost: ¥270,000)
Fiscal Year 2014: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
Fiscal Year 2013: ¥2,600,000 (Direct Cost: ¥2,000,000、Indirect Cost: ¥600,000)
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| Keywords | GPIアンカー型タンパク質 / 固体NMR / 肢再生 / 脂質二重膜 / 固体ＮＭＲ / 肢の再生 / GPIアンカー型蛋白質 |
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| Outline of Final Research Achievements |
Newt Prod1 is tethered to the cell membrane by a glycosylphosphatidylinositol(GPI) anchor. We clarified the role for the anchoring of Prod1 using synthetic mimic of GPI-anchored Prod1 by solid-state NMR, fluorescence microscopy, and DLS measurement. Anchoring to the membrane drastically reduced the motion of Prod1 which attributed to the aggregation formation of anchored Prod1 on membranes. Three dimensional structure of the anchored Prod1 was not affected by aggregates formation on the membranes. The aggregated anchored Prod1 easily interacted with the anchored Prod1 tethered on opposing membrane surfaces, inducing membrane adhesion. Anchoring to the membrane is one of the reasons of the aggregation and following cell adhesion, but the high affinity between Prod1 should be also required for these phenomena. Thus, our results strongly assert the role of anchor in the salamander-specific protein Prod1 in assisting the cell adhesion function in the limb regeneration process.
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