Development of a new method for identifying substrates of PPM1 phosphatase family
| Project/Area Number |
15K12738
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| Research Category |
Grant-in-Aid for Challenging Exploratory Research
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| Allocation Type | Multi-year Fund |
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| Research Field |
Biomolecular chemistry
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| Research Institution | Hokkaido University |
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Principal Investigator |
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| Project Period (FY) |
2015-04-01 – 2017-03-31
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| Project Status |
Completed (Fiscal Year 2016)
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| Budget Amount *help |
¥3,640,000 (Direct Cost: ¥2,800,000、Indirect Cost: ¥840,000)
Fiscal Year 2016: ¥1,820,000 (Direct Cost: ¥1,400,000、Indirect Cost: ¥420,000)
Fiscal Year 2015: ¥1,820,000 (Direct Cost: ¥1,400,000、Indirect Cost: ¥420,000)
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| Keywords | 酵素 / 脱リン酸化 / プロテインホスファターゼ / 基質 / 蛋白質 / 翻訳後修飾 / ホスファターゼ / ペプチドライブラリー |
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| Outline of Final Research Achievements |
Protein Phosphorylation and dephosphorylation is a key mechanism for regulation of protein functions. Human PPM1 phosphatase family is composed of 12 members that play important roles in wide variety of cellular responses, such as differentiation, cell cycle regulation, and metabolism. However, there is not a versatile method to find cellular targets and substrates for these phosphatases. In this study, we designed a new method for identifying substrates and demonstrated that this method is very effective.
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Report
(3 results)
Research Products
(10 results)
