Novel conjugation of the ubiquitin-like protein Atg8 and its biological significance
Project/Area Number |
26440052
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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 | Osaka University |
Principal Investigator |
OKAMOTO Noriko 大阪大学, 生命機能研究科, 特任講師(常勤) (90568750)
|
Co-Investigator(Renkei-kenkyūsha) |
OKAMOTO Koji 大阪大学, 生命機能研究科, 准教授 (40455217)
|
Project Period (FY) |
2014-04-01 – 2017-03-31
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Project Status |
Completed (Fiscal Year 2016)
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Budget Amount *help |
¥4,940,000 (Direct Cost: ¥3,800,000、Indirect Cost: ¥1,140,000)
Fiscal Year 2016: ¥1,170,000 (Direct Cost: ¥900,000、Indirect Cost: ¥270,000)
Fiscal Year 2015: ¥2,080,000 (Direct Cost: ¥1,600,000、Indirect Cost: ¥480,000)
Fiscal Year 2014: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
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Keywords | Atg8 / ユビキチン様タンパク質 / オートファジー / 翻訳後修飾 / タンパク質分解 / ミトコンドリア / 出芽酵母 / 膜ダイナミクス / 品質管理 |
Outline of Final Research Achievements |
Atg8 is a phospholipid-conjugated ubiquitin-like protein essential for autophagy. Using budding yeast, this study demonstrated that Atg8 is also conjugated to several proteins under selective mitochondrial degradation-inducing conditions. In addition, Asu1 (Atg8ylation substrate 1), an endoplasmic reticulum membrane protein, has been identified as a substrate for Atg8 conjugation. It is possible that Atg8ylation contributes to autophagy-dependent degradation of Asu1.
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Report
(4 results)
Research Products
(5 results)
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[Journal Article] Phospholipid methylation controls Atg32-mediated mitophagy and Atg8 recycling2015
Author(s)
Sakakibara K, Eiyama A, Suzuki SW, Sakoh-Nakatogawa M, Okumura N, Tani M, Hashimoto A, Nagumo S, Kondo-Okamoto N, Kondo-Kakuta C, Asai E, Kirisako H, Nakatogawa H, Kuge O, Takao T, Ohsumi Y, Okamoto K
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Journal Title
EMBO Journal
Volume: 34
Issue: 21
Pages: 2703-2719
DOI
Related Report
Peer Reviewed / Open Access / Int'l Joint Research / Acknowledgement Compliant
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