牛のパピローマウイルスE5のオンコタンパク質は,真空のH(+) -ATPアゼの16K成分に結合する
D J Goldstein1, M E Finbow, T Andresson
1Department of Pathology, Georgetown University, Washington, DC 20007.
Nature
|July 25, 1991
まとめ
牛のパピローマウイルス1型E5タンパク質は,真空のATPアゼ成分である16Kタンパク質に結合する. この陽子ポンプとの相互作用は,E5誘発の細胞変容中に観察された細胞の変化を説明する可能性がある.
科学分野:
- 分子生物学は分子生物学である.
- 細胞生物学 細胞生物学
- ウイルス学 ウイルス学 ウイルス学
背景:
- 牛のパピローマウイルス1型 (BPV-1) E5タンパク質は,重要な変容剤である.
- E5は内膜に局所化し,細胞タンパク質と相互作用する.
- E5は成長因子受容体のチロシンリン酸化を誘発する.
研究 の 目的:
- BPV-1 E5変換タンパク質に結合する細胞16Kタンパク質を識別する.
- 細胞変容におけるE5-16Kタンパク質相互作用の機能的意義を解明する.
主な方法:
- コイムノプレシピテーションは,相互作用するタンパク質を特定するための測定法です.
- 細胞コンパートメント内のタンパク質の局所化の分析.
- E5発現に反応する成長因子受容体のリン酸化の評価.
主要な成果:
- E5に関連した16Kタンパク質は,真空のATPases (v-ATPases) のサブユニットとして識別されました.
- この16K v-ATPase成分は,様々な水泡や膜複合体で見られる統合膜タンパク質です.
- 16K v-ATPaseタンパク質とのE5の相互作用は,成長因子受容体のリン酸化と相関しています.
結論:
- BPV-1 E5オンコタンパク質は,真空アテパースの16Kサブユニットと相互作用する.
- この相互作用は,エンドソームのコンパートメントの陽子ポンプの機能を妨害する可能性が高い.
- E5によるv-ATPase機能の破壊は,変換中に観察されたプレイオモルフな細胞変化の根底にある可能性があります.
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