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アセチル化がオートファギーの調節における機能と分子メカニズム
Cong Yi1, Meisheng Ma, Leili Ran
1State Key Laboratory of Biomembrane and Membrane Biotechnology, School of Life Sciences, Tsinghua University, Beijing, China.
Science (New York, N.Y.)
|April 28, 2012
まとめ
タンパク質アセチル化は,オートファギーを調節する. この研究では,ESA1がK19とK48でAtg3をアセチル化することを特定し,この細胞プロセスに不可欠なオートファギーのシグナル伝達とタンパク質相互作用を制御しました.
科学分野:
- 細胞生物学 細胞生物学
- 分子生物学は分子生物学である.
- バイオケミストリー バイオケミストリー
背景:
- タンパク質アセチル化は,細胞プロセスにおける重要な規制メカニズムである.
- 細胞の基本的なプロセスであるオートファギーは,様々な生理学的および病理学的状態に関与しています.
- ヒストンアセチルトランスフェラーゼ (HAT) とデアセチラーゼは,遺伝子発現とタンパク質機能の調節に重要な役割を果たします.
研究 の 目的:
- タンパク質アセチル化がオートファギーの調節における役割を調査する.
- アセチル化の標的であるオートファギーに関与する特定のタンパク質を特定する.
- アセチル化がオートファギーのシグナル伝達と実行を制御するメカニズムを解明する.
主な方法:
- Saccharomyces cerevisiae.の遺伝子解析について
- オートファギータンパク質のアセチルライシン残留物の特定.
- タンパク質とタンパク質の相互作用とタンパク質の脂質化に関する分析.
- 飢餓中の酵素の局所化と活性に関する研究.
主要な成果:
- ヒストンアセチルトランスフェラーゼであるEsa1は,オートファジーに不可欠であると特定されました.
- オートファギーのシグナル伝達成分であるAtg3は,K19とK48.8でEsa1アセチル化のための基質であることが判明しました.
- K19-K48におけるAtg3のアセチル化は,Atg3-Atg8の相互作用とAtg8の脂化を調節することによって,オートファギーを調節する.
- 飢餓は,前自体構造におけるEsa1とRpd3の空間時間的調節を通じた一時的なAtg3アセチル化を誘導する.
- アセチル化の減衰は,オートファギーの減少と相関しており,Rpd3の削除はアセチル化とオートファギーを増加させた.
結論:
- タンパク質アセチル化,特にK19-K48のAtg3は,オートファギーの重要な調節因子である.
- アセチラゼEsa1とデアセチラゼRpd3の相互作用は,オートファギーの動態を制御する.
- この研究は,翻訳後の改変とオートファギーの調節を結びつける新しいメカニズムを明らかにしています.
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