Analysis of molecular mechanisms of Akt-mediated cell polarity regulation.
| Project/Area Number |
25440039
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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 biochemistry
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| Research Institution | Hokkaido University |
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Principal Investigator |
Suizu Futoshi 北海道大学, 遺伝子病制御研究所, 講師 (90431379)
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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 |
¥5,330,000 (Direct Cost: ¥4,100,000、Indirect Cost: ¥1,230,000)
Fiscal Year 2015: ¥1,040,000 (Direct Cost: ¥800,000、Indirect Cost: ¥240,000)
Fiscal Year 2014: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
Fiscal Year 2013: ¥2,860,000 (Direct Cost: ¥2,200,000、Indirect Cost: ¥660,000)
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| Keywords | 細胞極性 / 一次繊毛 / Akt / 嚢胞腎 / リン酸化 / 基質 |
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| Outline of Final Research Achievements |
We have tried to identify the new Akt substrate in primary cilia as a factor for controlling cell polarity based on a hypothesis for Akt to participate in structure maintenance of primary cilia. By using the Yeast Hybrid System method, we used Akt2 and Akt3 isoform as a bait, respectively. As a result, we have succeeded in isolating and identifying primary cilia protein Inversin which was both isolated by Akt2 and Akt3 screening. Inversin bound to all of Akt1, 2 and 3 isoforms, but other Ser-Thr kinase (PDK or PrkA), suggesting that it was the Akt specific binding factor. Furthermore, we made it clear that Inversin was new Akt substrate and we identified its phosphorylation sites. The phosphorylation is indispensable to lumen-like structure in the three-dimensional culture of the canine MDCK cells; meaning that the phosphorylation signal transduction via Akt-Inversin plays an important role for controlling cell polarity and body plan of vertebrates.
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Report
(4 results)
Research Products
(15 results)
