Regulation of the Bfa1p-Bub2p complex at spindle pole bodies by the cell cycle phosphatase Cdc14p.
Regulation of the Bfa1p-Bub2p complex at spindle pole bodies by the cell cycle phosphatase Cdc14p.
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DOI：
10.1083/jcb.200112085
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发表时间：
2002-04-29
期刊：
影响因子：
--
通讯作者：
Schiebel E
中科院分区：
文献类型：
--
作者：
Pereira G;Manson C;Grindlay J;Schiebel E
芽殖酵母有丝分裂退出网络（MEN）是一个由GTP酶驱动的信号转导级联反应，它控制后期核仁中磷酸酶Cdc 14 p的释放，从而驱动有丝分裂退出。我们发现，Cdc 14 p是部分释放的核仁在早期后期独立的行动的MEN组件Cdc 15 p，Dbf 2 p，和Tem 1 p。在释放时，Cdc 14 p通过与Bfa 1 p-Bub 2 p GTdR激活蛋白复合物结合到纺锤体极体（SPB），已知Bfa 1 p-Bub 2 p GTdR激活蛋白复合物调节G蛋白Tem 1 p的活性。Cdc 14 p也与这种GT3相互作用。MEN组分Mob 1 p与SPB的结合作为MEN活化的标志物。Cdc 14 p和Mob 1 p在后期早期同时结合SPB表明Cdc 14 p最初激活MEN。在第二个，稍后的步骤，这符合有丝分裂退出，Cdc 14 p重新激活Bfa 1 p-Bub 2 p复合物通过去磷酸化Bfa 1 p。这使MEN失活并从SPB中置换Mob 1 p。这些数据表明，Cdc 14 p激活的MEN在后期早期，但后来失活，通过Bfa 1 p去磷酸化，因此限制MEN活动在后期的一个短时期。
The budding yeast mitotic exit network (MEN) is a GTPase-driven signal transduction cascade that controls the release of the phosphatase Cdc14p from the nucleolus in anaphase and thereby drives mitotic exit. We show that Cdc14p is partially released from the nucleolus in early anaphase independent of the action of the MEN components Cdc15p, Dbf2p, and Tem1p. Upon release, Cdc14p binds to the spindle pole body (SPB) via association with the Bfa1p–Bub2p GTPase activating protein complex, which is known to regulate the activity of the G protein Tem1p. Cdc14p also interacts with this GTPase. The association of the MEN component Mob1p with the SPB acts as a marker of MEN activation. The simultaneous binding of Cdc14p and Mob1p to the SPB in early anaphase suggests that Cdc14p initially activates the MEN. In a second, later step, which coincides with mitotic exit, Cdc14p reactivates the Bfa1p–Bub2p complex by dephosphorylating Bfa1p. This inactivates the MEN and displaces Mob1p from SPBs. These data indicate that Cdc14p activates the MEN in early anaphase but later inactivates it through Bfa1p dephosphorylation and so restricts MEN activity to a short period in anaphase.
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