Molecular regulatory mechanisms for post-translational modifications of the water channel controlling salivary secretion.
| Project/Area Number |
25462891
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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 |
Functional basic dentistry
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| Research Institution | The University of Tokushima |
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Principal Investigator |
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| Co-Investigator(Kenkyū-buntansha) |
YOSHIMURA Hiroshi 徳島大学, 大学院医歯薬学研究部, 教授 (90288845)
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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: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
Fiscal Year 2014: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2013: ¥2,210,000 (Direct Cost: ¥1,700,000、Indirect Cost: ¥510,000)
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| Keywords | アクアポリン / 翻訳後修飾 / リン酸化 / ユビキチン化 / 細胞内膜輸送 / 唾液腺 / アクアポリン5 / 細胞内シグナル伝達 |
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| Outline of Final Research Achievements |
We investigated the post-translational modifications, short-chain ubiquitination and phosphorylation, of water channel aquaporin-5 (AQP5). Ca2+-induced AQP5 ubiquitination in human salivary gland cells may not play critical roles in the intracellular trafficking events, such as endocytosis, recycling, uptake into multivesicular bodies, and secretion. Although the roles of these modifications could not be fully elucidated in the present study, we identified two ubiquitin ligases for AQP5 ubiquitination and some AQP5 binding proteins, which may be a phosphorylation-dependent. In addition, we found little direct interactions between phosphorylation and ubiquitination of AQP5.
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Report
(4 results)
Research Products
(2 results)
