| Budget Amount *help |
¥576,680,000 (Direct Cost: ¥443,600,000、Indirect Cost: ¥133,080,000)
Fiscal Year 2011: ¥116,350,000 (Direct Cost: ¥89,500,000、Indirect Cost: ¥26,850,000)
Fiscal Year 2010: ¥116,350,000 (Direct Cost: ¥89,500,000、Indirect Cost: ¥26,850,000)
Fiscal Year 2009: ¥116,350,000 (Direct Cost: ¥89,500,000、Indirect Cost: ¥26,850,000)
Fiscal Year 2008: ¥111,280,000 (Direct Cost: ¥85,600,000、Indirect Cost: ¥25,680,000)
Fiscal Year 2007: ¥116,350,000 (Direct Cost: ¥89,500,000、Indirect Cost: ¥26,850,000)
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| Research Abstract |
Our study was performed by focusing two issues in protein quality control in the endoplasmic reticulum (ER). The first one was on the productive folding of nascent polypeptides by molecular chaperones and oxidoredcutases in the ER. The second one was to reveal the quality control mechanism of ER-associated degradation (ERAD) system that eliminates the misfolded proteins from the ER. We found two novel factors involved in the ERAD, EDEM1 and ERdj5. In this term, mainly three issues on this proposal was addressed: 1) we succeeded to solve the crystal structure of ERdj5 that reduces the disulfide bonds in the misfolded proteins to be degraded and proposed the substrate transfer pathway in the ERAD system for glycoproteins, 2) we revealed the novel ERAD pathway for misfolded non-glycosylated proteins, and 3) we showed the electron transfer pathway in the process of oxidation including Ero1a, PDI and ERp46.
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