p34cdc2関連タンパク質キナーゼによるp60c-srcのミトーシス固有のリン酸化
D O Morgan1, J M Kaplan, J M Bishop
1Department of Microbiology, University of California, San Francisco 94143.
Cell
|June 2, 1989
まとめ
細胞分裂中のスレオニンにp60c-srcをリン酸化する新しいミトーシス特異のタンパク質キナーゼ. このキナーゼの活動はp34cdc2と関連しており,p60c-srcがミトーシスのp34cdc2エフェクタとして作用することを示唆しています.
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:
- タンパク質チロシンキナーゼであるp60c-srcは,ミトーシス過程で,そのアミノ末端領域でスレオニンリン酸化を受けます.
- この特定のミト酸性リン酸化に起因するキナーゼを特定することは,細胞循環調節を理解するために極めて重要です.
研究 の 目的:
- p60c-srcのミトーシス特異的なスレオニンリン酸化に責任を負うタンパク質キナーゼを特定し,特徴づけること.
- このキナーゼ活性と既知のミトーシス調節体,特にp34cdc2.2.の関係を調べる.
主な方法:
- HeLa細胞とXenopus卵からのミト細胞抽出物は,キナーゼ活性を探すために使用されました.
- 浄化されたp60c-srcを用いたインビトロリン酸化アッセイが実施された.
- トリプティックフォスフォペプチドマッピングは,リン酸化部位を分析するために使用されました.
- ゲルフィルタレーションクロマトグラフィは,キナーゼコンミグレーションを評価するために使用されました.
- p34cdc2に対する抗体を用いた免疫低下が実施されました.
主要な成果:
- HeLa細胞とXenopus卵でミトーシス特異のタンパク質キナーゼ活性が特定され,p60c-srcをスレオニン残基にリン酸化する能力がある.
- フォスフォペプチドマッピングにより,同定されたキナーゼが,ミトーシス中にインビヴォで改変された場所と同じ部位をリン酸化することを確認しました.
- ミトスのヘラキナーゼ活性がp34cdc2関連ヒストンH1キナーゼと結合した.
- p34cdc2に対する抗体は,ミトーシス抽出物からp60c-src-phosphorylating活動を枯渇させた.
結論:
- 結果は,スレオニンでp60c-srcをリン酸化する新しいミトーシス特異キナーゼを特定した.
- このキナーゼの活動はp34cdc2と関連しており,機能的なリンクが示唆されています.
- p60c-srcは,特定のミトーシスプロセスにおけるp34cdc2のエフェクタとして機能し,細胞サイクル調節に貢献する可能性があります.
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