Substrate recognition mechanism of the endoplasmic reticulum-localized mannosidase EDEM
Project/Area Number |
15K06996
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Research Category |
Grant-in-Aid for Scientific Research (C)
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Allocation Type | Multi-year Fund |
Section | 一般 |
Research Field |
Functional biochemistry
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Research Institution | Kyoto University |
Principal Investigator |
Okada Tetsuya 京都大学, 理学研究科, 助教 (70378529)
|
Project Period (FY) |
2015-04-01 – 2018-03-31
|
Project Status |
Completed (Fiscal Year 2017)
|
Budget Amount *help |
¥5,070,000 (Direct Cost: ¥3,900,000、Indirect Cost: ¥1,170,000)
Fiscal Year 2017: ¥910,000 (Direct Cost: ¥700,000、Indirect Cost: ¥210,000)
Fiscal Year 2016: ¥1,820,000 (Direct Cost: ¥1,400,000、Indirect Cost: ¥420,000)
Fiscal Year 2015: ¥2,340,000 (Direct Cost: ¥1,800,000、Indirect Cost: ¥540,000)
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Keywords | タンパク質分解 / マンノシダーゼ / 小胞体 / 小胞体関連分解 / 糖鎖 / マンノース |
Outline of Final Research Achievements |
Mannose trimming in the endoplasmic reticulum required for glycoprotein degradation is carried out by the EDEM family proteins (EDEM 1/2/3). In this study, we clarified the functional significance of EDEM2 in the mannose trimming reaction and identified three cysteine residues essential for the mannosidase activity of EDEM2. We also identified an candidate for the partner protein of EDEM2. In addition, we found that severely misfolded glycoproteins are forcibly degraded even in the absence of EDEM-mediated mannose trimming.
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Report
(4 results)
Research Products
(4 results)
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[Journal Article] Forcible destruction of severely misfolded mammalian glycoproteins by the non-glycoprotein ERAD pathway.2015
Author(s)
Ninagawa S, Okada T, Sumitomo Y, Horimoto S, Sugimoto T, Ishikawa T, Takeda S, Yamamoto T, Suzuki T, Kamiya Y, Kato K, Mori K.
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Journal Title
The Journal of Cellular Biology
Volume: 211
Issue: 4
Pages: 775-784
DOI
NAID
Related Report
Peer Reviewed / Open Access / Acknowledgement Compliant
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