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首页> 外文期刊>Cell cycle >Cell cycle phosphorylation of mitotic exit network (MEN) proteins.
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Cell cycle phosphorylation of mitotic exit network (MEN) proteins.

机译:有丝分裂出口网络(MEN)蛋白的细胞周期磷酸化。

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摘要

Phosphorylation of proteins is an important mechanism used to regulate most cellular processes. Recently, we completed an extensive phosphoproteomic analysis of the core proteins that constitute the Saccharomyces cerevisiae centrosome. Here, we present a study of phosphorylation sites found on the mitotic exit network (MEN) proteins, most of which are associated with the cytoplasmic face of the centrosome. We identified 55 sites on Bfa1, Cdc5, Cdc14 and Cdc15. Eight sites lie in cyclin-dependent kinase motifs (Cdk, S/T-P), and 22 sites are completely conserved within fungi. More than half of the sites were found in centrosomes from mitotic cells, possibly in preparation for their roles in mitotic exit. Finally, we report phosphorylation site information for other important cell cycle and regulatory proteins.
机译:蛋白质的磷酸化是用于调节大多数细胞过程的重要机制。最近,我们完成了对构成酿酒酵母中心体的核心蛋白的广泛磷酸化蛋白质组学分析。在这里,我们介绍有丝分裂出口网络(MEN)蛋白质上发现的磷酸化位点的研究,其中大多数与中心体的细胞质表面有关。我们在Bfa1,Cdc5,Cdc14和Cdc15上确定了55个站点。八个位点位于细胞周期蛋白依赖性激酶基序(Cdk,S / T-P)中,而22个位点在真菌内完全保守。在有丝分裂细胞的中心体中发现了超过一半的位点,可能是为它们在有丝分裂出口中的作用做准备。最后,我们报告了其他重要细胞周期和调控蛋白的磷酸化位点信息。

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