Roles of the organelle-specific ubiquitination regulators in protein degradation
Project/Area Number |
24570209
|
Research Category |
Grant-in-Aid for Scientific Research (C)
|
Allocation Type | Multi-year Fund |
Section | 一般 |
Research Field |
Cell biology
|
Research Institution | Tokyo Institute of Technology |
Principal Investigator |
|
Project Period (FY) |
2012-04-01 – 2015-03-31
|
Project Status |
Completed (Fiscal Year 2014)
|
Budget Amount *help |
¥5,070,000 (Direct Cost: ¥3,900,000、Indirect Cost: ¥1,170,000)
Fiscal Year 2014: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
Fiscal Year 2013: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
Fiscal Year 2012: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
|
Keywords | ユビキチン / タンパク質分解 / 小胞体 / ミトコンドリア / ユビキチン化 / 脱ユビキチン化酵素 / 脱ユビキチン |
Outline of Final Research Achievements |
Although protein quality control is essential for maintaining cellular function, its molecular mechanism is not fully understood. In this study, we performed the characterization of the endoplasmic-reticulum (ER) deubiquitinating enzyme USP19 and showed that USP19 stabilizes the ER-associated ubiquitinating enzyme MARCH6 via deubiquitination. It is known that MARCH6 has a role in protein quality control in the ER. In addition, the stabilization of MARCH6 increases its enzymatic activity and thereby promotes degradation of the mutant ABCB11, a substrate of MARCH6. These results suggest that USP19 is involved in the regulation of protein quality control in the ER.
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Report
(4 results)
Research Products
(10 results)