| Project/Area Number |
23590100
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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 |
Biological pharmacy
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| Research Institution | Himeji Dokkyo University |
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Principal Investigator |
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| Co-Investigator(Kenkyū-buntansha) |
SHIRAKI Takashi 姫路獨協大学, 薬学部, 准教授 (10294208)
SAKAI Nobuya 姫路獨協大学, 薬学部, 講師 (30525077)
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| Co-Investigator(Renkei-kenkyūsha) |
KOSHIMIZU Taka-aki 自治医科大学, 医学部, 准教授 (20392491)
IMANISHI Yorihisa 慶應義塾大学, 医学部, 講師 (80255538)
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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: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2012: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2011: ¥2,210,000 (Direct Cost: ¥1,700,000、Indirect Cost: ¥510,000)
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| Keywords | Ｓａｖ１ / 分子シャペロン / アグレソーム / ミトコンドリア / 細胞周期 / 上皮間葉転換 / ユビキチン化 |
|---|
| Research Abstract |
Using high throughput proteomics screening, we identified the molecular chaperones (Hsp60 and Hsp70) as a novel protein associated with Sav1 (mammalian homologue of Salvador). Sav1 targets to the aggresome and its sequestration to the aggresome is enhanced by the proteasome inhibitor MG132. Furthermore, Sav1 co-localized with Hsp70 and CHIP (carboxy terminus of Hsp70-interacting protein) that has been shown to mediate substrate ubiquitination and degradation by the proteasome. In addition, anti-Sav1 immunostainings displayed partial colocalization with Hsp60. In this study, we demonstrate that Hsp60 is one of the proteins that binds to Sav1. The interaction between Hsp60 and Sav1 could influence the Hsp60-mediated signaling cascade. This study suggest that Sav1 has a previously unexpected critical role in the aggresome pathway.
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