Regulation of ER-localized mannosidase EDEM2 via the intermolecular disulfide bond
| Project/Area Number |
18K06110
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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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| Review Section |
Basic Section 43030:Functional biochemistry-related
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| Research Institution | Kyoto University |
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Principal Investigator |
Okada Tetsuya 京都大学, 理学研究科, 助教 (70378529)
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| Project Period (FY) |
2018-04-01 – 2021-03-31
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| Project Status |
Completed (Fiscal Year 2020)
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| Budget Amount *help |
¥4,420,000 (Direct Cost: ¥3,400,000、Indirect Cost: ¥1,020,000)
Fiscal Year 2020: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
Fiscal Year 2019: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
Fiscal Year 2018: ¥1,820,000 (Direct Cost: ¥1,400,000、Indirect Cost: ¥420,000)
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| Keywords | 小胞体 / マンノシダーゼ / タンパク分解 / 小胞体関連分解 / タンパク質分解 / 糖鎖 |
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| Outline of Final Research Achievements |
Mannose trimming of N-glycan regulates endoplasmic reticulum (ER)-associated degradation of misfolded glycoproteins. In this study, we found that EDEM2, a putative ER-localized mannosidase, was stably disulfide-bounded to TXNDC11, an ER-localized protein with five thioredoxin-like domains. This covalent association was essential for mannose trimming and glycoprotein degradation. We also clearly demonstrated for the first time that EDEM2-TXNDC11 complex purified from culture cells had mannosidase activity against N-glycan in vitro.
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| Academic Significance and Societal Importance of the Research Achievements |
本研究によるEDEM2-TXNDC11複合体のマンノシダーゼ活性検出により、遺伝子破壊解析の知見から我々が提唱していた小胞体のマンノース刈り込みの分子機構が生化学的にも立証された。小胞体における不要タンパク質の分解は、細胞の生命活動において不可欠な機構である。TXNDC11によるEDEM2の活性制御の発見とEDEMタンパク質の酵素活性の測定法の確立により、その分子機構の理解がより深まると期待される。
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Report
(4 results)
Research Products
(4 results)
