Elucidation of the physiological function of novel E3 ubiquitin ligase that induces the inactivation of constitutively active proteins by the proteasome-dependent degradation
| Project/Area Number |
26460068
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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 |
Biological pharmacy
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| Research Institution | Ohu University |
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Principal Investigator |
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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: ¥1,040,000 (Direct Cost: ¥800,000、Indirect Cost: ¥240,000)
Fiscal Year 2015: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2014: ¥2,470,000 (Direct Cost: ¥1,900,000、Indirect Cost: ¥570,000)
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| Keywords | ECS(SPSB1/2/4) / ECS(SPSB3) / CDC14A / Nrf3 / ユビキチン化 / タンパク質分解 / ECS(SPSB) / SPSB3 / iNOS / NQO1 / SPSB / FOG-2 / CTTNBP2 |
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| Outline of Final Research Achievements |
We showed that CDC14A, a dual-specificity protein phosphatase, was polyubiquitinated by ECS(SPSB1/2/4) E3 ligase complex and degraded by the 26S proteasome. Additionally, we identified Nrf3 as a substrate for ECS(SPSB3). We found that ECS(SPSB3) induces the polyubiquitination of Nrf3 through the binding to the C-terminal region of Nrf3 and negatively regulates the function of Nrf3.
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Report
(4 results)
Research Products
(4 results)
