分泌されたチロシンキナーゼは,細胞外環境で作用する
Mattia R Bordoli1, Jina Yum2, Susanne B Breitkopf3
1Department of Developmental Biology, Harvard School of Dental Medicine, Boston, MA 02115, USA.
Cell
|August 30, 2014
まとめ
研究者らは,新しい分泌タンパク質チロシンキナーゼであるVascular Like Kinase (VLK) を発見した. この発見は,細胞外チロシンリン酸化がイン・ビヴォで広範囲に及んでおり,組織調節におけるチロシンリン酸化の役割も説明できる.
科学分野:
- バイオケミストリー バイオケミストリー
- 細胞生物学 細胞生物学
- 分子生物学は分子生物学である.
背景:
- 細胞外タンパク質の広範な in vivo タイロシンリン酸化が観察されていますが,分泌されるタンパク質タイロシンキナーゼの責任者は未特定です.
- 特定された分泌タンパク質チロシンキナーゼの欠如は,組織調節における細胞外チロシンリン酸化の役割に関する研究を妨げています.
研究 の 目的:
- 細胞外タンパク質のリン酸化を司る分泌タンパク質チロシンキナーゼを特定する.
- 細胞外環境における特定されたキナーゼの機能と基板を調査する.
主な方法:
- 血管のようなキナーゼ (VLK) のキナーゼ活性を特徴付けるために生化学的アッセイを使用しました.
- 刺激を受けたときに血小板からVLKの分泌を調査した.
- VLKの分泌およびER定住タンパク質に対する基板特異性を評価した.
- VLK媒介のリン酸化におけるATP源の役割を調べた.
主要な成果:
- Vascular Like Kinase (VLK) は,分泌されるタンパク質チロシンキナーゼとして特定されました.
- VLKは,分泌およびER居住基板タンパク質の多様な配列をリン酸化する.
- VLKは刺激に対する反応として,血小板から迅速かつ定量的に分泌されます.
- VLKは,内生性ATPと外生性ATPの両方を用いてタンパク質をリン酸化することができる.
結論:
- VLKの発見は,広範囲に広がる in vivo 細胞外チロシンリン酸化の分子基盤を提供します.
- VLKは,調節されたチロシンリン酸化の重要性を細胞外環境に拡張します.
- VLKは,細胞外信号伝達による生理学的および病理学的組織調節を理解するために重要である.
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