CDK依存のHsp70リン酸化は,G1サイクリン濃度と細胞サイクル進行を制御する
Andrew W Truman1, Kolbrun Kristjansdottir, Donald Wolfgeher
1Ludwig Center for Metastasis Research, The University of Chicago, Chicago, IL 60637, USA.
Cell
|December 11, 2012
まとめ
サイクリン依存キナーゼ (CDK) による熱ショックタンパク質70 (Hsp70) リン酸化は,G1サイクリン安定性と細胞サイクル進行を制御する. このメカニズムは,ヒトに保存され,サイクリン豊富さと活動を調節することによって成長を調節します.
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:
- Hsp70チャペロンは,細胞機能を調節する重要なタンパク質です.
- 彼らの活動は,発現,同型,およびコチャペロンによって調節されます.
研究 の 目的:
- Hsp70機能の新たな規制メカニズムを調査する.
- 細胞サイクル制御におけるHsp70リン酸化の役割を調査する.
主な方法:
- 芽生える酵母におけるリン酸化部位分析 Ssa1.1.
- Ssa1,Ydj1,Cln3.3の相互作用を調査する
- Ssa1のリン酸化とCln3の安定性に対するCDK Pho85とCdk1の影響を研究する.
- 人間のHsc70とサイクリンD1.1.における保存型リン酸化を検証する.
主要な成果:
- CDKによるT36におけるSsa1のリン酸化は,コチャペロンとクライアントの相互作用を変化させる.
- T36のリン酸化はYdj1を位移させ,Ssa1がG1サイクリンCln3.3を結合して分解することを可能にします.
- ストレスとミトーシスのCDK (Pho85,Cdk1) は,Ssa1のリン酸化を介してCln3の安定性を調節する.
- 人間のHsc70 T38のCDK依存型リン酸化は,サイクリンD1の安定性に影響を及ぼします.
結論:
- Hsp70は,細胞成長制御における信号変換器として作用します.
- CDK媒介のHsp70のリン酸化により,G1サイクリンの豊富性と活性が調節される.
- このリン酸化機構は酵母から人間に保存されます.
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