| Budget Amount *help |
¥4,940,000 (Direct Cost: ¥3,800,000、Indirect Cost: ¥1,140,000)
Fiscal Year 2017: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
Fiscal Year 2016: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
Fiscal Year 2015: ¥1,950,000 (Direct Cost: ¥1,500,000、Indirect Cost: ¥450,000)
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| Outline of Final Research Achievements |
Protein phosphorylation is strictly regulated by protein kinases and protein phosphatases, and disordered regulation of protein phosphorylation often causes serious disease, such as cancer. It is important to identify substrates for Ser/Thr phosphatases to clarify the signal transduction and disease mechanisms, however, there are still no their reliable methods. Here, we developed two novel substrate-identification methods for Ser/Thr phosphatases, one is method termed Phosphorylation Mimic Phage Display (PMPD), to identify substrate for SCP1 phosphatase using peptide phage display libraries with Mg2+ and AlF4- and another is development of substrate trapping mutants for PPM1D phosphatase. These methods can be useful and applicable for other Ser/Thr phosphatases.
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