Quantitative phosphoproteomics analysis of the TORC1 signaling

细胞控制细胞的生长和增殖以响应营养。雷帕霉素复合物1（TORC 1）蛋白激酶的靶标是该营养负责系统的中心，并调节各种细胞事件以响应营养。然而，下游事件的全貌在很大程度上是未知的。我们之前已经证明，当细胞用特异性TORC 1抑制剂雷帕霉素处理时，大量蛋白质被降解，这表明TORC 1通过磷酸化介导蛋白质降解。因此，研究TORC 1失活对哪些蛋白磷酸化有影响具有重要意义。在这里，我们进行了定量磷酸化组学分析来剖析这个问题。我们发现，雷帕霉素处理后，许多蛋白质的磷酸化水平增加或减少。

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.