Genetic and biochemical analysis of the ER quality control of membrane proteins
Project/Area Number |
18K19306
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Research Category |
Grant-in-Aid for Challenging Research (Exploratory)
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Allocation Type | Multi-year Fund |
Review Section |
Medium-sized Section 43:Biology at molecular to cellular levels, and related fields
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Research Institution | Nagoya City University |
Principal Investigator |
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Project Period (FY) |
2018-06-29 – 2022-03-31
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Project Status |
Completed (Fiscal Year 2021)
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Budget Amount *help |
¥6,370,000 (Direct Cost: ¥4,900,000、Indirect Cost: ¥1,470,000)
Fiscal Year 2020: ¥2,080,000 (Direct Cost: ¥1,600,000、Indirect Cost: ¥480,000)
Fiscal Year 2019: ¥1,820,000 (Direct Cost: ¥1,400,000、Indirect Cost: ¥420,000)
Fiscal Year 2018: ¥2,470,000 (Direct Cost: ¥1,900,000、Indirect Cost: ¥570,000)
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Keywords | 小胞体 / 膜タンパク質 / ユビキチン / プロテアソーム / 分解 |
Outline of Final Research Achievements |
Misfolded or unassembled proteins in the endoplasmic reticulum (ER) are degraded by the proteasome. This process is referred to as ER-associated degradation or ERAD. In this study, we analyzed the mechanisms of membrane protein degradation during ERAD: (1)Experimental and theoretical analysis to predict membrane protein insertion in yeast cells; (2)Physiological role of the ERAD of membrane proteins; (3)Genetic analysis of the retrotranslocation complex. (4)We also performed collaborative research to study ERAD in mammals.
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Academic Significance and Societal Importance of the Research Achievements |
細胞には立体構造の形成に失敗した異常タンパク質を特異的に認識して分解する品質管理の仕組みが備わっている。本研究では、小胞体の膜に存在する異常タンパク質に着目し、出芽酵母の遺伝学、生化学の手法を駆使して、分解の仕組みを詳細に解析した。本研究で得られた成果は、異常タンパク質の蓄積を防ぐ方法論の開発につながるものと期待される。
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Report
(5 results)
Research Products
(22 results)
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[Journal Article] Hepatic Sdf2l1 controls feeding-induced ER stress and regulates metabolism2019
Author(s)
Sasako T., Ohsugi M., Kubota N., Itoh S., Okazaki Y, Terai A., Kubota T., Yamashita S., Nakatsukasa K., Kamura T., Iwayama K., Tokuyama K., Kiyonari H., Furuta Y., Shibahara J., Fukayama M., Enooku K., Okushin K., Tsutsumi T., Tateishi R., Tobe K., Asahara H., Koike K., *Kadowaki T. & *Ueki K.
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Journal Title
Nature Communications
Volume: 10
Issue: 1
Pages: 1-16
DOI
Related Report
Peer Reviewed / Open Access
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