2015 Fiscal Year Final Research Report
The mechanisms of A20-mediated control of cIAP1 and its involvement in diseases.
| Project/Area Number |
25460356
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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 |
General medical chemistry
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| Research Institution | Chiba University |
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Principal Investigator |
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| Project Period (FY) |
2013-04-01 – 2016-03-31
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| Keywords | シグナル伝達 / ユビキチン |
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| Outline of Final Research Achievements |
The ubiquitin editing enzyme A20 is composed of an N-terminal OTU domain and 7 C-terminal zinc finger motifs (ZnFs). A20 functions as a de-ubiquitinating enzyme through the OTU domain and as an ubiquitin E3 ligase through the 4th ZnF. A20 suppresses activation of the transcription factor NF-κB in an enzymatic activity-dependent manner. In this study, A20 was found to directly bind to another ubiquitin E3 ligase cIAP1 through the 7th ZnF (ZnF7) and induce activation of NF-κB and suppression of apoptosis by controlling cIAP1. Because ZnF7 is frequently mutated in B-cell lymphoma, defects in control of cIAP1 by A20 may be involved in progression of this disease.
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| Free Research Field |
分子生物学
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