Analysis of how misfolded proteins are delivered to retrotranslocation complex for ER-associated degradation
| Project/Area Number |
18K06216
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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 44010:Cell biology-related
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| Research Institution | Kyoto University |
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Principal Investigator |
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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: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2018: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
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| Keywords | 小胞体関連分解 / 構造異常タンパク質 / N型糖鎖 / マンノーストリミング / 糖鎖 / レクチン / OS-9 / XTP3B / オルガネラゾーン / OS-9/XTP3B |
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| Outline of Final Research Achievements |
In the endoplasmic reticulum (ER) secretory and membrane proteins are synthesized. During the synthesis, some proteins cannot fold properly. Such misfolded proteins are degraded via proteasome in the cytosol. In this study, I focus on how misfolded proteins are delivered from ER lumen to ER membrane and revealed the redundant roles of OS9 and XTP3B for substrate degradation.
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| Academic Significance and Societal Importance of the Research Achievements |
本研究成果は、小胞体の構造異常タンパク質がどのように分解されるかを明らかにすることを主眼としている。その成果として糖鎖依存分解経路の中心因子であるOS9とXTP3Bの機能的な重複が分かった。これにより、アルツハイマー病やパーキンソン病をはじめとする60以上ものヒトの疾患と関わると報告されたこの小胞体関連分解機構の分子メカニズムの一端を明らかにすることができた。将来的に、ヒト疾患への新たな治療法や予防法につながる可能性がある。
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Report
(4 results)
Research Products
(17 results)
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[Journal Article] Improved secretion of glycoproteins using an N-glycan-restricted passport sequence tag recognized by cargo receptor2020
Author(s)
Yagi H., Yagi-Utsumi M., Honda R., Ohta Y., Saito T., Nishio M., Ninagawa S., Suzuki K., Anzai T., Kamiya Y., Aoki K., Nakanishi M., Satoh T., Kato K.
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Journal Title
NATURE COMMUNICATIONS
Volume: 11
Pages: 1368-1368
DOI
Related Report
Peer Reviewed / Open Access / Int'l Joint Research
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