Funational analysis of Rfu1 that regulates ubiquitin homeostasis
| Project/Area Number |
23570184
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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 |
Functional biochemistry
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| Research Institution | Tokyo Metropolitan Institute of Medical Science |
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Principal Investigator |
KIMURA Yoko 公益財団法人東京都医学総合研究所, 生体分子先端研究分野, 主任研究員 (80291152)
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| Project Period (FY) |
2011 – 2013
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| Project Status |
Completed (Fiscal Year 2013)
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| Budget Amount *help |
¥5,330,000 (Direct Cost: ¥4,100,000、Indirect Cost: ¥1,230,000)
Fiscal Year 2013: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
Fiscal Year 2012: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
Fiscal Year 2011: ¥1,950,000 (Direct Cost: ¥1,500,000、Indirect Cost: ¥450,000)
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| Keywords | ユビキチン / エンドソーム / Bro1 / Rfu1 / 蛋白質分解 / ユビキチンリガーゼ / 脱ユビキチン化酵素 / ホメオスタシス / Rsp5 / ubiquitin / 熱ショックストレス / endosome / Alix |
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| Research Abstract |
Yeast Rfu1 (Regulator for free ubiquitin chain 1) localizes to endosomes and plays a role in ubiquitin homeostasis by inhibiting the activity of Doa4. We showed that Bro1 that recruits Doa4 to endosomes and stimulates Doa4 deubiquitinating activity, also recruits Rfu1 to endosomes. This recruitment is mediated by a direct interaction between the YPEL motif in the Rfu1 carboxyl-terminus and the V domain in Bro1. Furthermore, overexpression of Bro1, particularly the V domain, prevents Rfu1 degradation in response to heat shock. Thus, Bro1 regulates both the localization and stability of Rfu1. Rfu1 degradation involved the proteasome and a ubiquitin ligase Rsp5, suggesting that Rfu1 stability is regulated by ubiquitin-proteasome pathways.
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Report
(4 results)
Research Products
(28 results)
