| Project/Area Number |
25850244
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| Research Category |
Grant-in-Aid for Young Scientists (B)
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| Allocation Type | Multi-year Fund |
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| Research Field |
Applied molecular and cellular biology
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| Research Institution | Kagawa University |
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Principal Investigator |
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| Project Period (FY) |
2013-04-01 – 2015-03-31
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| Project Status |
Completed (Fiscal Year 2014)
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| Budget Amount *help |
¥4,290,000 (Direct Cost: ¥3,300,000、Indirect Cost: ¥990,000)
Fiscal Year 2014: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2013: ¥2,730,000 (Direct Cost: ¥2,100,000、Indirect Cost: ¥630,000)
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| Keywords | Pcdh-gc5 / CaMKP / CaMKP-N / phosphorylation / dephosphorylation / protocadherin / CaM kinase |
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| Outline of Final Research Achievements |
Ca2+/CaM-dependent protein kinase phosphatase (CaMKP/PPM1F) is a Ser/Thr protein phosphatase that belongs to the PPM family. In this study, we identified CaMKP binding proteins, including protocadherin gamma subfamily C5 (Pcdh-γC5), that interacted with the N-terminal region of CaMKP using E. coli two-hybrid system. To identify the responsible region of interaction, we prepared deletion mutants of CaMKP and Pcdh-γC5. GST-pull down assay with Pcdh-γC5(715-944), a cytoplasmic tail of Pcdh-γC5, revealed that CaMKP(1-98) is responsible for the interaction. Although Pcdh-γC5(715-944) itself did not affect on the phosphatase activity of CaMKP, dephosphorylation of Phospho-CaMKI by CaMKP was found to be significantly promoted in the presence of Pcdh-γC5 (715-944) both in vitro and in cells. Taken together, these results strongly suggest that Pcdh-γC5(715-944) can act as a scaffold for CaMKP and CaMKI to regulate CaMKP activity.
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