The mitotic peptidyl-prolyl isomerase, Pin1, interacts with Cdc25 and Plx1
The mitotic peptidyl-prolyl isomerase, Pin1, interacts with Cdc25 and Plx1
复制标题
DOI：
10.1093/emboj/17.5.1315
复制
发表时间：
1998-03-02
期刊：
影响因子：
11.4
通讯作者：
Kornbluth, S
中科院分区：
文献类型：
--
作者：
Crenshaw, DG;Yang, J;Kornbluth, S
顺式/反式肽基脯氨酰异构酶，Pin 1，是一个调节有丝分裂，是很好地保守从酵母man. In这里，我们证明了从爪蟾卵提取物的Pin 1结合蛋白的耗竭导致过度磷酸化和失活的关键有丝分裂调节，Cdc 2/细胞周期蛋白B。我们表明，这种表型是一个后果Pin 1相互作用的关键上游调控Cdc 2/细胞周期蛋白B，包括Cdc 2-定向磷酸酶，Cdc 25，和它的已知调节，Plx 1。虽然Pint可以在间期和有丝分裂过程中与Plx 1相互作用，但只有磷酸化的有丝分裂活性形式的Cdc 25能够结合Pin 1，我们使用体外磷酸化Cdc 25重现了这一事件。综上所述，这些数据表明，Pin 1可能通过与Cdc 25及其激活剂Plx 1相互作用来调节细胞周期控制。
The cis/trans peptidyl-prolyl isomerase, Pin1, is a regulator of mitosis that is well conserved from yeast to man. Here we demonstrate that depletion of Pin1-binding proteins from Xenopus egg extracts results in hyperphosphorylation and inactivation of the key mitotic regulator, Cdc2/cyclin B. We show biochemically that this phenotype is a consequence of Pin1 interaction with critical upstream regulators of Cdc2/cyclin B, including the Cdc2-directed phosphatase, Cdc25, and its known regulator, Plx1. Although Pint could interact with Plx1 during interphase and mitosis, only the phosphorylated, mitotically active form of Cdc25 was able to bind Pin1, an event we have recapitulated using in vitro phosphorylated Cdc25. Taken together, these data suggest that Pin1 may modulate cell cycle control through interaction with Cdc25 and its activator, Plx1.