Regulating mechanism for intracellular stability of tyrosine hydroxylase and neurodegeneration
| Project/Area Number |
22590946
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Neurology
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| Research Institution | Fujita Health University |
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Principal Investigator |
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| Co-Investigator(Kenkyū-buntansha) |
OTA Akira 藤田保健衛生大学, 医学部, 教授 (10247637)
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| Co-Investigator(Renkei-kenkyūsha) |
HAYASHI Nobuhiro 東京工業大学, 生命理工学研究科 (80267955)
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| Project Period (FY) |
2010 – 2012
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| Project Status |
Completed (Fiscal Year 2012)
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| Budget Amount *help |
¥2,990,000 (Direct Cost: ¥2,300,000、Indirect Cost: ¥690,000)
Fiscal Year 2012: ¥650,000 (Direct Cost: ¥500,000、Indirect Cost: ¥150,000)
Fiscal Year 2011: ¥910,000 (Direct Cost: ¥700,000、Indirect Cost: ¥210,000)
Fiscal Year 2010: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
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| Keywords | 神経分子病態学 / パーキンソン病 / チロシン水酸化酵素 / 細胞内安定性 / プロテアソーム分解 / 14-3-3プロテイン / リン酸化 / 細胞内安定性制御機構 |
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| Research Abstract |
We revealed that the phosphorylation of the N-terminal portion of tyrosine hydroxylase (TH) positively regulates the intracellular stability of the enzyme. The phosphorylation of two serine residues was shown to be a trigger for the proteasomedigestion. Moreover, 14-3-3 protein which is major protein in mammalian brain is a critical factor in regulating TH stability by acting to promote the degradation of TH phosphorylated at its N-terminus.
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Report
(4 results)
Research Products
(16 results)
