近日，IDIBELL研究人员确定了蛋白质Zds1片断在有丝分裂中发挥关键作用。
Bellvitge生物医学研究所（IDIBELL）研究人员发现蛋白质Zds1在有丝分裂过程中发挥关键性作用的机制。相关研究论文发表在Journal of Cell Science杂志上，这一研究取得的结果为发展靶向性癌症疗法铺平了道路。
每一个有机体中，细胞生长和分裂成两个子细胞的过程被称为“细胞周期”。细胞必须完成细胞周期过程中四个主要步骤：G1和G2期、对数生长期（S期）、染色体的分离（M期、有丝分裂期）和分裂期（细胞分裂）。在S期或是DNA复制期，遗传物质进行复制，在M期或有丝分裂过程中，细胞之间染色体分开复制成两个子细胞。
染色体的稳定性
遗传信息（DNA），从父到子（或从细胞到细胞）的传输是生物学上的基本问题。非整倍体，即染色体的缺乏或过剩，是几乎所有人类癌症类型中的特征。有规律的有丝分裂对维持染色体的稳定性尤为重要。
然而，尽管DNA很重要性，但很少有人知道有丝分裂产生的确切结果。这项发表在Journal of Cell Sciencs杂志的文章中，IDIBELL研究细胞周期的小组由埃塞尔Queralt领导，研究发现新的有丝分裂的调控机制。
Separase蛋白是一种染色体分离和有丝分裂调控的重要组成部分。Queralt博士首次描述了Zds1蛋白参与保持染色体完好性，Zds1蛋白与Separase一起确保细胞到细胞之间正确的基因遗传。
研究人员表示蛋白质Zds1调节有丝分裂和染色体分离的分子机制需进行深入研究。本文采用一种模式生物酵母来开展研究。（生物谷：Bioon.com）
doi:10.1242/jcs.097865
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Zds1 regulates PP2ACdc55 activity and Cdc14 activation during mitotic exit via its Zds_C motif
Ines Calabria, Barbara Baro, Jose-Antonio Rodriguez-Rodriguez, Nuria Russi?ol and Ethel Queralt*
At anaphase onset, highly active mitotic cyclin-dependent kinase (Cdk) is inactivated to promote exit from mitosis and completion of cytokinesis. The budding yeast Cdc14p phosphatase is a key mitotic regulator that counteracts cyclin-dependent kinase (Cdk) activity during mitotic exit. Separase, together with Zds1p, promotes the down-regulation of PP2ACdc55 in early anaphase, enabling accumulation of phosphorylated forms of Net1p and nucleolar release of Cdc14p. Here we show that the C-terminal domain of Zds1p, called the Zds_C motif, is required for Zds1-induced release of Cdc14p, while the N-terminal domain of the protein might be involved in regulating this activity. More interestingly, Zds1p physically interacts with Cdc55p, and regulates its localization via the Zds_C motif. Nevertheless, expression of the Zds_C motif at endogenous levels cannot induce timely nucleolar release of Cdc14, despite the proper (nucleolar) localization of Cdc55p. Our results suggest that the activity of PP2ACdc55 cannot be modulated solely through regulation of its localization, and that an additional regulatory step may be required. These results suggest that Zds1p recruits PP2ACdc55 to the nucleolus and induces its inactivation by an unknown mechanism.
