Regulation of synaptic plasticity by receptor-like protein tyrosine phosphatase
| Project/Area Number |
21700416
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| Research Category |
Grant-in-Aid for Young Scientists (B)
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| Allocation Type | Single-year Grants |
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| Research Field |
Neurochemistry/Neuropharmacology
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| Research Institution | National Institute for Basic Biology |
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Principal Investigator |
FUJIKAWA Akihiro National Institute for Basic Biology, 統合神経生物学研究部門, 特別協力研究員 (50414016)
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| Project Period (FY) |
2009 – 2010
|
| Project Status |
Completed (Fiscal Year 2010)
|
| Budget Amount *help |
¥4,290,000 (Direct Cost: ¥3,300,000、Indirect Cost: ¥990,000)
Fiscal Year 2010: ¥1,820,000 (Direct Cost: ¥1,400,000、Indirect Cost: ¥420,000)
Fiscal Year 2009: ¥2,470,000 (Direct Cost: ¥1,900,000、Indirect Cost: ¥570,000)
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| Keywords | 神経科学 / 生体分子 / 蛋白質 / 脳・神経 |
|---|
| Research Abstract |
The extracellular region of Ptprz is shedded by MMP-9 or plasmin, producing its membrane-tethered fragment. Both proteases are reportedly activated when synaptic remodeling is occurring. We revealed that Ptprz fragments are accumulated in the post synaptic density PSD fraction, indicating that this receptor is actually cleaved at central synapses. We identified the dephosphorylation sites in Git1 and Magi1. Alignment of the primary sequences surrounding the target phospho-tyrosine residue in these substrate proteins showed a considerable similarity, suggesting a consensus motif for substrate recognition by Ptprz. We found that the substrate motif thus deduced is present in some proteins, including at Tyr118 of paxillin. Finally, we verified that Ptprz efficiently dephosphorylates paxillin at this site in cultured cells.
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Report
(3 results)
Research Products
(6 results)
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[Book] 細胞工学2011
Author(s)
藤川顕寛・野田昌晴
Total Pages
5
Publisher
学研メディカル秀潤社
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