Physiological role of reducing redox state near membrane in ER protein quality control
Project/Area Number |
26440050
|
Research Category |
Grant-in-Aid for Scientific Research (C)
|
Allocation Type | Multi-year Fund |
Section | 一般 |
Research Field |
Functional biochemistry
|
Research Institution | Kyoto University |
Principal Investigator |
Hoseki Jun 京都大学, 農学研究科, 特任准教授 (40423058)
|
Project Period (FY) |
2014-04-01 – 2017-03-31
|
Project Status |
Completed (Fiscal Year 2016)
|
Budget Amount *help |
¥5,200,000 (Direct Cost: ¥4,000,000、Indirect Cost: ¥1,200,000)
Fiscal Year 2016: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2015: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2014: ¥2,080,000 (Direct Cost: ¥1,600,000、Indirect Cost: ¥480,000)
|
Keywords | レドックス / 小胞体 / グルタチオン |
Outline of Final Research Achievements |
We have developed ERroGFP S4 which could visualize ER redox states and elucidated the mechanism by which an ER disulfide reductase, ERdj5 received reductive power in an oxidative environment of the ER and promoted degradation of misfolded proteins. We found that ERdj5 is localized near ER membrane where the redox state is more reducing than that in the ER lumen. Therefore, ERdj5 efficiently received reductive power of reduced glutathione derived from cytosol and promoted ERAD.
|
Report
(4 results)
Research Products
(13 results)