ミトーシス中のSH2およびSH3ドメインを通じてSrcに関連付けられたRNA結合タンパク質
1Section of Biochemistry, Molecular and Cell Biology, Cornell University, Ithaca, New York 14853.
Nature
|April 28, 1994
まとめ
ミトーシス中の活性化されたc-Srcキナーゼは,68Kタンパク質 (p68) をリン酸化し,結合する. これは,c-Srcが細胞サイクル中にRNAの処理,輸送,または翻訳を調節することを示唆しています.
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:
- c-Srcチロシンキナーゼの活動は,脱酸化経由でミトーシス中に増加する.
- ミトスのc-Src活性化により,Srcホモロジー-2 (SH2) ドメイン結合が強化される.
- ミトスのc-Srcの生理学的標的は,ほとんど特定されていないままです.
研究 の 目的:
- ミトーシス中の活性化c-Srcの生理学的標的を特定する.
- c-Srcとそのミトーシス標的との相互作用を調査する.
主な方法:
- ミトーシス中のマウスの線維芽細胞におけるチロシンリン酸化測定.
- タンパク質とタンパク質の相互作用を検出するための共免疫プレシピテーション.
- Src SH2およびSH3ドメインを使用したインビトロ結合アッセイ.
- p68タンパク質ホモロジーと結合相手の分析.
主要な成果:
- A68Kタンパク質 (p68) はチロシン・リン酸化され,ミトーシス過程でSrcと結合する.
- p68はSrcのSH2およびSH3ドメインにインビトロで独立して結合する.
- SH2とSH3ドメインは,p68のリン酸化と結合に不可欠である.
- p68は,ポリリボヌクレオチドを結合することが知られているp62とホモロジーを共有しています.
結論:
- ミトティックc-Srcはp68.8と直接相互作用し,それをリン酸化する.
- この相互作用は,c-Src.のSH2とSH3ドメインの両方を含む.
- c-Srcは,細胞サイクルに依存した方法でRNA関連のプロセス (処理,トランスレーション,トランスレーション) を調節する可能性があります.
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