| Budget Amount *help |
¥5,200,000 (Direct Cost: ¥4,000,000、Indirect Cost: ¥1,200,000)
Fiscal Year 2016: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2015: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2014: ¥2,080,000 (Direct Cost: ¥1,600,000、Indirect Cost: ¥480,000)
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| Outline of Final Research Achievements |
Newly synthesized proteins obtain its native conformations by the assistance of chaperone proteins and folding enzymes, while polypeptides that failed to fold correctly are disposed by the intracellular degradation machinery. This mechanism is named as protein quality control. Misfolded proteins are prone to aggregate, and accumulation of these abnormal species frequently impairs cellular function, causing conformational diseases.
In the present study, we analyzed the molecular mechanisms of protein quality control system in mammalian endoplasmic reticulum (ER), focusing on the proteins that inhibit aggregation formation in the ER, and the membrane complex in the ER that plays the central role in ER-associated protein degradation.
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