Elucidation of molecular mechanism of polyglutamine protein induced dysfunction of mitochondrial membrane and dynamics
| Project/Area Number |
23770108
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| Research Category |
Grant-in-Aid for Young Scientists (B)
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| Allocation Type | Multi-year Fund |
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| Research Field |
Structural biochemistry
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| Research Institution | Kurume University |
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Principal Investigator |
TADATO Ban 久留米大学, 分子生命科学研究所, 助教 (00579667)
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| Project Period (FY) |
2011 – 2012
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| Project Status |
Completed (Fiscal Year 2012)
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| Budget Amount *help |
¥4,290,000 (Direct Cost: ¥3,300,000、Indirect Cost: ¥990,000)
Fiscal Year 2012: ¥2,080,000 (Direct Cost: ¥1,600,000、Indirect Cost: ¥480,000)
Fiscal Year 2011: ¥2,210,000 (Direct Cost: ¥1,700,000、Indirect Cost: ¥510,000)
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| Keywords | 神経変性疾患 / ポリグルタミン蛋白質 / ミスフォールディング / アミロイド線維 / ミトコンドリア / 脂質膜 / 膜ダイナミクス / ポリグルタミン病 / プロテオリポソーム / 膜融合 / ポリグルタミン / 膜融合・分裂 / コンフォメーション変化 / 会合体形成 / リポソーム |
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| Research Abstract |
Polyglutamine disease is neurodegenerative disorder caused by protein misfolding and aggregation. In this study, we analyzed the effect of conformational change of model polyglutamine protein to its enzymatic function and interaction with model lipid membrane. We show the enzymatic activity of polyglutamine protein is suppressed by soluble amyloidogenic conformer. This finding indicates that conformational transitions of polyglutamine protein inhibit physiological function and induce cellular dysfunction.
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Report
(3 results)
Research Products
(2 results)
