Identification and functional analysis of substrates of disease-associated protein kinases using multiple phosphoproteomic technologies
| Project/Area Number |
26440101
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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 |
Cell biology
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| Research Institution | The University of Tokushima |
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Principal Investigator |
KOSAKO Hidetaka 徳島大学, 先端酵素学研究所(オープンイノベ), 教授 (10291171)
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| Co-Investigator(Renkei-kenkyūsha) |
MATSUDA Noriyuki 東京都医学総合研究所, 生体分子先端研究分野, プロジェクトリーダー (10332272)
NAKAYA Michio 九州大学, 薬学研究院, 准教授 (80464387)
ISHIZAKI Toshimasa 大分大学, 医学部, 教授 (70293876)
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| Project Period (FY) |
2014-04-01 – 2017-03-31
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| Project Status |
Completed (Fiscal Year 2016)
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| Budget Amount *help |
¥5,070,000 (Direct Cost: ¥3,900,000、Indirect Cost: ¥1,170,000)
Fiscal Year 2016: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2015: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
Fiscal Year 2014: ¥1,820,000 (Direct Cost: ¥1,400,000、Indirect Cost: ¥420,000)
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| Keywords | シグナル伝達 / プロテオーム / リン酸化 / キナーゼ / PINK1 / ERK / PKD / ユビキチン / T細胞 / 核膜孔複合体 / ROCK |
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| Outline of Final Research Achievements |
Many diseases are associated with mutations in protein kinases. To fully and therapeutically understand the complex signaling networks, it is essential to develop analytical strategies for the global identification and functional characterization of in vivo substrates of individual protein kinases. In this study, we have identified novel substrates of three disease-associated protein kinases including PINK1, ERK and PKD by using the IMAC/2D-DIGE method, Phos-tag Western blotting and mass spectrometry. Furthermore, we uncovered molecular mechanisms by which each kinase regulates cellular functions through these substrates.
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Report
(4 results)
Research Products
(15 results)
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[Journal Article] Ubiquitin is phosphorylated by PINK1 to activate parkin.2014
Author(s)
Koyano, F., Okatsu, K., Kosako, H., Tamura, Y., Go, E., Kimura, M., Kimura, Y., Tsuchiya, H., Yoshihara, H., Hirokawa, T., Endo, T., Fon. E. A., Trempe, J. F., Saeki, Y., Tanaka, K., and Matsuda, N.
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Journal Title
Nature
Volume: 510(in press)
Issue: 7503
Pages: 162-166
DOI
Related Report
Peer Reviewed
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