| Budget Amount *help |
¥5,460,000 (Direct Cost: ¥4,200,000、Indirect Cost: ¥1,260,000)
Fiscal Year 2013: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
Fiscal Year 2012: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
Fiscal Year 2011: ¥2,730,000 (Direct Cost: ¥2,100,000、Indirect Cost: ¥630,000)
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| Research Abstract |
Cells control cell growth and proliferation in response to nutrients. The target of rapamycin complex 1 (TORC1) protein kinase is the center of this nutrition-responsible system and regulates various cellular events in response to nutrition. However, the full view of downstream events is largely unknown. We have previously shown that when cells were treated with the specific TORC1 inhibitor rapamycin, a huge number of proteins were degraded, suggesting that TORC1 mediates protein degradation via phosphorylation. It is very important to disclose of which proteins phosphorylation is changed by TORC1 inactivation. Here we performed quantitative phosphoproeomics analysis to dissect this issue. We found that phosphorylation of a lot of proteins were increased or decreased after rapamycin treatment.
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