ティロシンベースの内細胞モチーフによって刺激されたシナプトタグミンへのAP-2の徴募
1Department of Cell Biology and Howard Hughes Medical Institute, Yale University School of Medicine, 295 Congress Avenue, New Haven, CT 06510, USA.
Science (New York, N.Y.)
|August 24, 1999
まとめ
貨物タンパク質は,AP-2がシナプトタグミンに結合することを強化することにより,クラトリン媒介性エンドサイトーシスを刺激します. このメカニズムは,プラズマ膜へのAP-2の徴募を促進し,クラトリンコーティングピット形成を開始します.
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:
- クラトリン媒介性内細胞症 (CME) は,分子内化のための重要な細胞プロセスです.
- アダプタータンパク質AP-2は,CMEを誘発するために,血に誘導されます.
- シナプトタグミンは,プラズマ膜のAP-2のドッキングサイトとして機能すると仮定されています.
研究 の 目的:
- CME中にAP-2の徴募を刺激する貨物タンパク質の役割を調査する.
- AP-2とシナプトタグミン,および内細胞モチーフの相互作用を解明する.
主な方法:
- タイロシンベースの内細胞性モチーフを含むペプチドを使用した.
- AP-2のシナプトタグミンへの結合を in vitroで評価した.
- ニューロン細胞および非ニューロン細胞におけるプラズマ膜へのAP-2の徴集を測定した.
主要な成果:
- タイロシンベースの内細胞性モチーフを持つペプチドは,シナプトタグミンへのAP-2結合を著しく強化した.
- これらのペプチドは,また,様々な細胞タイプにおけるプラズマ膜へのAP-2の徴集を促進しました.
- 貨物タンパク質モチーフとAP-2-シナプトタグミン相互作用の間の直接的なリンクが示されました.
結論:
- 貨物タンパク質の負荷は,クラスリンでコーティングされたピッツの核化を刺激します.
- AP-2とシナプトタグミンの間の相互作用は,貨物由来の内細胞性モチーフによって調節されます.
- これは,クラスリン媒介性エンドサイトーシスの負荷駆動的開始のための分子機構を提供します.
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