The role of an unstructured region in the proteasome inhibition
| Project/Area Number |
22770137
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| Research Category |
Grant-in-Aid for Young Scientists (B)
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| Allocation Type | Single-year Grants |
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| Research Field |
Functional biochemistry
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| Research Institution | University of Toyama (2011)
The Institute of Physical and Chemical Research (2010) |
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Principal Investigator |
INOBE Tomonao 富山大学, 先端ライフサイエンス拠点, 特命助教 (50568855)
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| Project Period (FY) |
2010 – 2011
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| Project Status |
Completed (Fiscal Year 2011)
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| Budget Amount *help |
¥4,290,000 (Direct Cost: ¥3,300,000、Indirect Cost: ¥990,000)
Fiscal Year 2011: ¥2,080,000 (Direct Cost: ¥1,600,000、Indirect Cost: ¥480,000)
Fiscal Year 2010: ¥2,210,000 (Direct Cost: ¥1,700,000、Indirect Cost: ¥510,000)
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| Keywords | 細胞内タンパク質分解 / プロテアソーム / ポリグルタミン病 / 神経変性疾患 / 天然変性蛋白質 / 蛋白質 / 分解 / ハンチントン病 / ハンチンチン / 蛋白質分解 / 天然変性領域 |
|---|
| Research Abstract |
We have investigated how the misfolded proteins in various neurodegenerative diseases inhibit the protein degradation by the proteasome. We found that an unstructured region of the misfolded protein directly interacts with the proteasome, which causes the competitive inhibition of the degradation of natural proteasome substrates and the disassembly of the 19S proteasome complex.
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Report
(3 results)
Research Products
(16 results)
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[Journal Article] Sequence-and Species-Dependence of Proteasomal Processivity2012
Author(s)
Kraut, DA., Israeli, E., Schrader, E., Patil, A., Nakai, K., Nanavati, D., Inobe, T. and Matouschek, A.
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Journal Title
ACS Chem. Biol.(in press)
Related Report
Peer Reviewed
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