| Project/Area Number |
25870312
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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 |
Functional biochemistry
Cell biology
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| Research Institution | Nagoya University |
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Principal Investigator |
NAKATSUKASA Kunio 名古屋大学, 理学(系)研究科(研究院), 助教 (90547522)
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| Project Period (FY) |
2013-04-01 – 2015-03-31
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| Project Status |
Completed (Fiscal Year 2014)
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| Budget Amount *help |
¥4,290,000 (Direct Cost: ¥3,300,000、Indirect Cost: ¥990,000)
Fiscal Year 2014: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
Fiscal Year 2013: ¥2,600,000 (Direct Cost: ¥2,000,000、Indirect Cost: ¥600,000)
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| Keywords | 小胞体 / タンパク質 / 品質管理機構 / ユビキチン / 分解 / 品質管理 / ユビキチンリガーゼ / タンパク質複合体 / 生体膜 |
|---|
| Outline of Final Research Achievements |
Inactivation of Cdc48p/p97 stalled retrotranslocation and triggered formation of a complex that contains the 26S proteasome, Cdc48p/p97, ubiquitinated substrates, select components of the Hrd1 complex, and the lumenal recognition factor, Yos9p. We proposed that the actions of Cdc48p/p97 and the proteasome are tightly coupled during ERAD. Our data also support a model in which the Hrd1 complex links substrate recognition and degradation on opposite sides of the ER membrane. Based on these results, we performed in vivo site-specific crosslinking experiments. Non-natural photo-reactive amino acids were incorporated into Hrd3 in yeast to detect cross-linked Hrd1. Although we could detect some cross-linked products with Hrd3, it is currently unclear if these are Hrd1-Hrd3 crosslinked products. We are now trying to scale up the system to better detect Hrd1. In addition, we are analyzing a role of the transmembrane domain of Hrd3 especially under the stress conditions.
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