Analysis of substrate-recognition mode by novel ubiquitin ligase related to endoplasmic reticulum-associated degradation pathway.
Project/Area Number |
21580121
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Research Category |
Grant-in-Aid for Scientific Research (C)
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Allocation Type | Single-year Grants |
Section | 一般 |
Research Field |
Applied biochemistry
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Research Institution | 財団法人東京都医学総合研究所 (2011) Tokyo Metropolitan Organization for Medical Research (2009-2010) |
Principal Investigator |
YOSHIDA Yukiko 財団法人東京都医学総合研究所, 生体分子先端研究分野, 主任研究員 (90271543)
|
Project Period (FY) |
2009 – 2011
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Project Status |
Completed (Fiscal Year 2011)
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Budget Amount *help |
¥4,940,000 (Direct Cost: ¥3,800,000、Indirect Cost: ¥1,140,000)
Fiscal Year 2011: ¥1,950,000 (Direct Cost: ¥1,500,000、Indirect Cost: ¥450,000)
Fiscal Year 2010: ¥1,950,000 (Direct Cost: ¥1,500,000、Indirect Cost: ¥450,000)
Fiscal Year 2009: ¥1,040,000 (Direct Cost: ¥800,000、Indirect Cost: ¥240,000)
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Keywords | F-box蛋白質 / ユビキチンリガーゼ / 小胞体関連分解 / N型糖鎖 / 基質認識 / 糖鎖 / 基質認識機構 |
Research Abstract |
We have reported previously that Fbs1 and Fbs2 are glycoprotein-specific F-box proteins, which are identified as the endoplasmic reticulum-associated degradation(ERAD)-linked ubiquitin ligase component. Here we report that Fbxo44b, which does not have sugar-binding activity, is involved in ubiquitylation of glycoproteins under the ERAD pathway. In addition, we analyzed the third F-box protein recognizing N-glycoproteins, Fbs3.Fbs3 can interact with glycoproteins modified with not only high-mannose but also complex-type glycans, suggesting that participates in unknown function of glycoproteins endocytosed from the cell surface but not through the ERAD pathway.
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Report
(4 results)
Research Products
(15 results)