| Budget Amount *help |
¥116,000,000 (Direct Cost: ¥116,000,000)
Fiscal Year 2011: ¥23,200,000 (Direct Cost: ¥23,200,000)
Fiscal Year 2010: ¥23,200,000 (Direct Cost: ¥23,200,000)
Fiscal Year 2009: ¥23,200,000 (Direct Cost: ¥23,200,000)
Fiscal Year 2008: ¥23,200,000 (Direct Cost: ¥23,200,000)
Fiscal Year 2007: ¥23,200,000 (Direct Cost: ¥23,200,000)
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| Research Abstract |
We analyzed the molecular mechanism of ER-associated degradation (ERAD). In addition to EDEM, which recruits the misfolded proteins from productive folding pathway to degradation pathway, we also found a novel reductase in the ER, ERdj5, is also involved in the acceleration of ERAD by cleaving disulfide bonds of the substrates. By using biochemical and structural analysis, we have revealed the substrate transfer pathway in the ERAD system; misfolded proteins are transferred from calnexin to EDEM1, ERdj5, BiP and finally to SEL1L in the ERAD complex.
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