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首页> 外文期刊>Cell cycle >Regulation of intracellular MEK1/2 translocation in mouse oocytes: cytoplasmic dynein/dynactin-mediated poleward transport and cyclin B degradation-dependent release from spindle poles.
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Regulation of intracellular MEK1/2 translocation in mouse oocytes: cytoplasmic dynein/dynactin-mediated poleward transport and cyclin B degradation-dependent release from spindle poles.

机译：小鼠卵母细胞中细胞内MEK1 / 2易位的调节：细胞质动力蛋白/动力蛋白介导的极向转运和细胞周期蛋白B降解依赖性从纺锤体极释放。

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摘要

We recently reported that MEK1/2 plays an important role in microtubule organization and spindle pole tethering in mouse oocytes, but how the intracellular transport of this protein is regulated remains unknown. In the present study, we investigated the mechanisms of poleward MEK1/2 transport during the prometaphase I/metaphase I transition and MEK1/2 release from the spindle poles during the metaphase I/anaphase I transition in mouse oocytes. Firstly, we found that p-MEK1/2 was colocalized with dynactin at the spindle poles. Inhibition of the cytoplasmic dynein/dynactin complex by antibody microinjection blocked polar accumulation of p-MEK1/2 and caused obvious spindle abnormalities. Moreover, coimmunoprecipitation of p-MEK1/2 and dynein or dynactin from mouse oocyte extracts confirmed their association at metaphase I. Secondly, disruption of microtubules by nocodazole resulted in the failure of poleward p-MEK1/2 transport. Whereas, when the nocodazole-treated oocytes were recovered in fresh culture medium, the spindle reformed and p-MEK1/2 relocalized to the spindle poles. Finally, we examined the mechanism of p-MEK1/2 release from the spindle poles. In control oocytes, polar p-MEK1/2 was gradually released during metaphase I/anaphase I transition. By contrast, in the presence of nondegradable cyclin B (Delta90), p-MEK1/2 still remained at the spindle poles at anaphase I. Our results indicate that poleward MEK1/2 transport is a cytoplasmic dynein/dynactin-mediated and spindle microtubule-dependent intracellular movement, and that its subsequent anaphase release from spindle poles is dependent on cyclin B degradation.
机译：我们最近报道，MEK1 / 2在小鼠卵母细胞中的微管组织和纺锤体极束缚中起着重要作用，但是如何调节这种蛋白的细胞内转运仍然未知。在本研究中，我们调查了小鼠卵母细胞中期I /中期I过渡期间向极点MEK1 / 2转运的机制和中期I /后期I过渡期间从纺锤极中释放的MEK1 / 2。首先，我们发现p-MEK1 / 2与动力蛋白在纺锤极共定位。抗体显微注射对细胞质动力蛋白/动力蛋白复合物的抑制作用会阻断p-MEK1 / 2的极性积累，并导致明显的纺锤体异常。此外，从小鼠卵母细胞提取物中对p-MEK1 / 2和dynein或dynactin的免疫共沉淀证实了它们在中期I的缔合。其次，诺考达唑对微管的破坏导致极向性p-MEK1 / 2转运失败。然而，当用诺考达唑处理的卵母细胞在新鲜培养基中回收时，纺锤体重新形成，p-MEK1 / 2重新定位到纺锤体极。最后，我们研究了p-MEK1 / 2从纺锤极释放的机理。在对照卵母细胞中，在中期I /后期I过渡过程中，极性p-MEK1 / 2逐渐释放。相比之下，在存在不可降解的细胞周期蛋白B（Delta90）的情况下，p-MEK1 / 2在后期I仍保留在纺锤体极点。我们的结果表明，向极的MEK1 / 2转运是细胞质动力蛋白/动力蛋白介导的纺锤体微管-依赖细胞内运动，其后续的后期释放从纺锤极取决于细胞周期蛋白B降解。

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