Proteomics of phospho-proteins during brain development using mutant mice
| Project/Area Number |
18500305
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Neurochemistry/Neuropharmacology
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| Research Institution | The Institute of Physical and Chemical Research |
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Principal Investigator |
OHSHIMA Toshio The Institute of Physical and Chemical Research, Laboratory for Developmental Neurobiology, Visiting Researcher (20311334)
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| Project Period (FY) |
2006 – 2007
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| Project Status |
Completed (Fiscal Year 2007)
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| Budget Amount *help |
¥4,020,000 (Direct Cost: ¥3,600,000、Indirect Cost: ¥420,000)
Fiscal Year 2007: ¥1,820,000 (Direct Cost: ¥1,400,000、Indirect Cost: ¥420,000)
Fiscal Year 2006: ¥2,200,000 (Direct Cost: ¥2,200,000)
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| Keywords | protein phosphorvlation / proteomics / 2D-DIGE / mutant mice / MS analysis / Cdk5 / stathmin / CRMP / Dab1 |
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| Research Abstract |
Purpose and Method : In this proposal, I attempt to understand the mechanism of brain development by analyzing protein phosphorylations which are important for such processes. Comparison of phospho-proteins between controls and mutant mice which have defective brain development will provide us new findings about molecular mechanism of brain development. For this purpose, we conducted 2D-DIGE method followed by MS analysis to identify the proteins.
Results: In 2006, we analyzed the cerebral cortex samples from Cdk5 KO mice and their littermate controls at E 18.5. Cdk5 is a neuron-specific Ser/Thr protein kinase and Cdk5 KO mice exhibit defective brain development particularly in layer formation of cortical structures. We conducted protetomics of phospho-proteins by 2D-DIGE method, and identified CRMP1, 2 and 4 among 23 differential spots. We previously reported that Cdk5 phosphorylates CRMP2 at Ser522. We confirmed that Cdk5 phosphorylates CRMP1 at Thr 509 in vivo using phosphor-specific antibody for pThr509 CRMP1. However, we couldn't detect the reduction of phosphorylation of CRMP4 Ser522, indicating the redundant phosphorylation by other kinase (s). We also found the reduced phosphorylation of stathmin Ser38 (Hayashi, et. al., 2006).
In 2007, we analyzed cerebella from Dab 1 mutant yotari and cerebellum-specific Cdk5 KO mice along with their littermate controls. We identified several differential spots and further analysis of these spots is now on going in our laboratory. We also reported that Cdk5 inhibits Reelin signaling through the phosphorylation of Dabl (Ohshima, et. al., 2007).
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Report
(3 results)
Research Products
(8 results)
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[Journal Article] Phosphorylation of the tubulin binding protein, stathmin by Cdk5 and MAP kinase in the brain.2006
Author(s)
Hayashi, K., Pan, Y., Shu, H., Ohshima, T., Kansy, W. J., White, CL., Tamminga, C. A., Sobel, A., Curmi, P. A., Mikoshiba, K., Bibb J. A.
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Journal Title
J. Neurochem. 99
Pages: 237-250
Description
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