Dbf2-Mob1 drives relocalization of protein phosphatase Cdc14 to the cytoplasm during exit from mitosis.
Dbf2-Mob1 drives relocalization of protein phosphatase Cdc14 to the cytoplasm during exit from mitosis.
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DOI：
10.1083/jcb.200812022
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发表时间：
2009-02-23
期刊：
影响因子：
--
通讯作者：
Deshaies RJ
中科院分区：
文献类型：
--
作者：
Mohl DA;Huddleston MJ;Collingwood TS;Annan RS;Deshaies RJ
有丝分裂结束的特征是细胞周期蛋白依赖性激酶（Cdk）活性急剧下降，有丝分裂结构溶解，细胞分裂。在酿酒酵母中，有丝分裂的退出是由一种蛋白磷酸酶Cdc14驱动的，该酶在一定程度上负责抵消Cdk活性。在整个间期，Cdc14被隔离在核仁中，但成功的后期激活有丝分裂出口网络（MEN），其触发Cdc14在整个细胞中的扩散机制尚不清楚。在这项研究中，我们发现MEN的一个组成部分，蛋白激酶Dbf2-Mob1，通过直接磷酸化Cdc14在核定位信号（NLS）附近的丝氨酸和苏氨酸残基上，从而促进Cdc14转移到细胞质并随后退出有丝分裂，从而取消其NLS活性。我们的结果确定了一种机制，MEN促进有丝分裂退出。
Exit from mitosis is characterized by a precipitous decline in cyclin-dependent kinase (Cdk) activity, dissolution of mitotic structures, and cytokinesis. In Saccharomyces cerevisiae, mitotic exit is driven by a protein phosphatase, Cdc14, which is in part responsible for counteracting Cdk activity. Throughout interphase, Cdc14 is sequestered in the nucleolus, but successful anaphase activates the mitotic exit network (MEN), which triggers dispersal of Cdc14 throughout the cell by a mechanism that has remained unknown. In this study, we show that a MEN component, protein kinase Dbf2–Mob1, promotes transfer of Cdc14 to the cytoplasm and consequent exit from mitosis by direct phosphorylation of Cdc14 on serine and threonine residues adjacent to a nuclear localization signal (NLS), thereby abrogating its NLS activity. Our results define a mechanism by which the MEN promotes exit from mitosis.
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DOI：
10.1073/pnas.0405925102
发表时间：
2005-04-12
影响因子：
11.1
作者：
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通讯作者：
Bloom, KS
影响因子：
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作者：
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影响因子：
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作者：
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通讯作者：
Deshaies, Raymond J.
影响因子：
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作者：
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通讯作者：
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影响因子：
11.4
作者：
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