MARCKSは,タンパク質キナーゼCとカルシウムカルモジュリンによって調節されるアクチンフィラメントクロスリンクタンパク質です
J H Hartwig1, M Thelen, A Rosen
1Department of Medicine, Brigham and Women's Hospital, Boston, Massachusetts.
Nature
|April 16, 1992
まとめ
タンパク質キナーゼC (PKC) は,重要な細胞骨格のタンパク質であるアクチンに影響することで細胞の形状を調節する. ミリスチル化され,アラニンに富んだCキナーゼ基板 (MARCKS) タンパク質は,PKCをアクチン組織に結合し,その活動はリン酸化とカルモジュリンによって調節されます.
科学分野:
- 細胞生物学 細胞生物学
- バイオケミストリー バイオケミストリー
- 分子生物学は分子生物学である.
背景:
- タンパク質キナーゼC (PKC) アゴニストは,細胞形態とアクチン組織を変化させます.
- ミリスチル化,アラニン豊富なCキナーゼ基板 (MARCKS) は,細胞運動に関与する特定のPKC基板です.
- PKCとアクチンアセンブリの間の直接的なリンクは確立されていません.
研究 の 目的:
- PKCシグナル伝達とアクチン細胞骨格の調節を結びつけるMARCKSの役割を調査する.
- MARCKSがPKC,カルモジュリン,アクチンとの架け橋として機能するかどうかを判断する.
主な方法:
- MARCKSのF-アクチンクロスリンク活性を評価するための生化学分析.
- PKC媒介によるリン酸化が,MARCKSの活性に及ぼす影響を調査する.
- MARCKSの機能に対するカルシウム-カルモジュリン結合の影響を調べる.
主要な成果:
- MARCKSは,糸状 (F) アクチンクロスリンクタンパク質として特定されました.
- PKC媒介によるリン酸化は,MARKSのアクチンクロスリンク活性を抑制する.
- カルシウム-カルモジュリン結合は,MARCKSのアクチンクロスリンク活性も抑制する.
結論:
- MARCKSは,アクチンとプラズマ膜の間の制御されたクロスブリッジとして機能します.
- カルモジュリンとリン酸化によるMARCKS活動の調節は,カルシウム-カルモジュリンとPKCシグナル伝達経路を統合する.
- これは,細胞信号への反応としてアクチン細胞骨格を調節するメカニズムを提供します.
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