| Project/Area Number |
25460376
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Multi-year Fund |
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| Section | 一般 |
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| Research Field |
General medical chemistry
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| Research Institution | Kanazawa Medical University |
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Principal Investigator |
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| Co-Investigator(Renkei-kenkyūsha) |
NAKAMURA Yuka 金沢医科大学, 総合医学研究所, 助手 (00565632)
TOMOSUGI Naohisa 金沢医科大学, 総合医学研究所, 教授 (80155580)
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| Project Period (FY) |
2013-04-01 – 2016-03-31
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| Project Status |
Completed (Fiscal Year 2015)
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| Budget Amount *help |
¥5,070,000 (Direct Cost: ¥3,900,000、Indirect Cost: ¥1,170,000)
Fiscal Year 2015: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2014: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
Fiscal Year 2013: ¥1,820,000 (Direct Cost: ¥1,400,000、Indirect Cost: ¥420,000)
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| Keywords | Y14 / 中心体 / リン酸化 / PhosTagゲル / RBM8A(Y14) / M期 / アポトーシス / RBM8A（Y14) |
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| Outline of Final Research Achievements |
Y14-Magohcomplex is a component of the exon junction complex (EJC) required for mRNA metabolism. However, the detailed status and mechanism of the phosphorylation of Y14 is poorly understood. We analyzed in detail Y14 phosphorylation in human cells. Phos-tag gels revealed that the majority of endogenous Y14 was phosphorylated throughout the cell-cycle progression. Nuclear and cytoplasmic Y14 and Y14 in the EJC was also found to be mostly phosphorylated. We also screened the phosphorylated serine by mutational analysis using Phos-tag gels to reveal modifications of serine residues 166 and 168. A single substitution at position 168 that concomitantly abolished the phosphorylation of serine 166 suggested the priority of kinase reaction between these sites. Furthermore, analysis of the role of the binding protein Magoh in Y14 phosphorylation revealed its inhibitory effect in vitro and in vivo.
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