2016 Fiscal Year Final Research Report
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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| Keywords | ECS(SPSB1/2/4) / ECS(SPSB3) / CDC14A / Nrf3 / ユビキチン化 / タンパク質分解 |
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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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| Free Research Field |
医歯薬学
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