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転写因子Stat91のインターフェロンの活性化には,SH2-フォスフォチロシルペプチド相互作用による二分化が含まれます
K Shuai1, C M Horvath, L H Huang
1Laboratory of Molecular Cell Biology, Rockefeller University, New York, New York 10021.
Cell
|March 11, 1994
まとめ
シグナルトランスデューサーとトランスクリプションのアクティベーター91 (Stat91) モノメアは,インターフェロン-ガンマ刺激で二元化します. SH2-フォスフォチロシル相互作用によって媒介されるこのStat91二分化は,DNA結合と遺伝子転写に不可欠です.
科学分野:
- 分子生物学は分子生物学である.
- 細胞シグナル伝達 細胞信号伝達
- 遺伝子規制 遺伝子規制
背景:
- シグナルトランスデューサーおよびトランスクリプションアクティベーター91 (Stat91) は,細胞質タンパク質である.
- Stat91は,インターフェロン-アルファおよびインターフェロン-ガンマなどのポリペプチド結合体への反応として,リン酸化によって活性化されます.
- 不活性なStat91は,細胞プラズマにモノマーとして存在します.
研究 の 目的:
- Stat91の活性化メカニズムを調査する.
- その機能におけるStat91二分化の役割を決定する.
- Stat91の二分化を媒介する分子相互作用を解明する.
主な方法:
- Stat91の局所化と活動を研究するための細胞アッセイ.
- Stat91.1.の酸化分析について
- タンパク質の相互作用を研究するための解離および再結合アッセイ.
- DNA結合アッセイ. DNA結合アッセイ.
主要な成果:
- インターフェロン-ガンマはStat91のリン酸化と安定したホモジマー形成を誘導する.
- Stat91ジマーだけが特定のDNA配列に結合して直接転写する.
- Stat91の二酸化は,SH2-phosphotyrosylペプチド相互作用によって媒介されます.
結論:
- Stat91の活性化には,SH2-phosphotyrosylの相互作用による二酸化が含まれています.
- Stat91の二分化は,DNA結合と転写活性化に不可欠である.
- この二分化メカニズムは,転写複合体における他のSTATタンパク質相互作用のモデルとして役立つかもしれない.
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