Control of mammalian circadian clock through phosphorylation-dependent proteolysis of Cry1
| Project/Area Number |
25830146
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| Research Category |
Grant-in-Aid for Young Scientists (B)
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| Allocation Type | Multi-year Fund |
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| Research Field |
System genome science
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| Research Institution | The University of Tokyo |
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Principal Investigator |
ODE Koji 東京大学, 医学(系)研究科(研究院), 助教 (40612122)
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| Project Period (FY) |
2013-04-01 – 2015-03-31
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| Project Status |
Completed (Fiscal Year 2014)
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| Budget Amount *help |
¥4,290,000 (Direct Cost: ¥3,300,000、Indirect Cost: ¥990,000)
Fiscal Year 2014: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
Fiscal Year 2013: ¥2,600,000 (Direct Cost: ¥2,000,000、Indirect Cost: ¥600,000)
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| Keywords | 概日時計 / 質量分析 / リン酸化 / Cry1 / FAD |
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| Outline of Final Research Achievements |
By introducing mutations on the phosphorylation sites of CRY1, one of the core component of mammalian circadian clock, many of these residues were found to be important for proper circadian period and/or robust amplitude both in cultured cell and mice. Analysis of the mutation effect on CRY1 properties re-emphasizes close coupling between CRY1 turnover rate and the circadian period. This relationship are rigorously tested by applying small-molecule-inducible degradation of CRY1.
Nevertheless, several mutants show markedly altered circadian period but less alter the CRY1 stability. These mutations are located mostly around the FAD-binding pocket of cryptochrome. We further confirmed that residues not directly linked to phosphorylation/electron-transferring but supposed to be retain the structure of the two domain also alter the period.
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Report
(3 results)
Research Products
(10 results)
