AAA-ATPase Cdc48/p97は,ミトーシスの終わりにスパインドルの分解を調節する
Kan Cao1, Reiko Nakajima, Hemmo H Meyer
1Department of Embryology, Carnegie Institution of Washington and Howard Hughes Medical Institute, Baltimore, MD 21210, USA.
Cell
|November 26, 2003
まとめ
AAA-ATPase Cdc48/p97チャペロン複合体は,ミトーシス・スパインドルの分解に不可欠である. この複合体は微小管の動態を調節し,細胞がミトーシスからインターフェーズへの移行を可能にします.
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:
- ミトスのスパインドルの分解は,細胞サイクル進行に不可欠ですが,まだよく理解されていません.
- AAA-ATPase Cdc48/p97とそのアダプタ Ufd1-Npl4 は,膜密輸における役割で知られている.
- Cdc48/p97がミトスの脱出時に微小管の動態を調節する正確な機能は不明である.
研究 の 目的:
- Cdc48/p97-Ufd1-Npl4がミトーシス・スパインドル分解における役割を調査する.
- ミトーシスの終わりにCdc48/p97-Ufd1-Npl4が微小管の動態を調節するメカニズムを解明する.
- スピンドルの解体のために,Cdc48/p97の機能が種間で保存されているかどうかを判断する.
主な方法:
- Xenopusの卵のエキスを利用して,spindleの分解を in vitroで研究しました.
- ホモログCdc48.8.を研究するために酵母に遺伝子解析を行った.
- Cdc48/p97-Ufd1-Npl4のスパインドル組立因子への直接結合を調査した.
主要な成果:
- Cdc48/p97-Ufd1-Npl4は,Xenopusの卵抽出物におけるミトスのスパインドルの分解に不可欠である.
- Cdc48/p97-Ufd1-Npl4機能の喪失は,固有の単極スパインドルの結果となり,インターフェーズマイクロチューブル配列の形成を妨げます.
- p97の酵母ホモログであるCdc48も,スパインドルの分解には必要である.
- Cdc48/p97-Ufd1-Npl4は,ミクロチューブル相互作用を調節し,スパインドル組成因子と直接相互作用する.
結論:
- Cdc48/p97-Ufd1-Npl4は,ミトスの脱出時に微小管のダイナミクスの重要な調節体として作用する.
- このチャプロン複合体は,細胞がインターフェーゼに戻るにつれて,マイクロチューブルの構造変化に不可欠です.
- スピンドルの解体におけるCdc48/p97の機能は,酵母からXenopus.に保存されています.
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