The midbody interactome reveals new unexpected roles for PP1 phosphatases in cytokinesis
The midbody interactome reveals new unexpected roles for PP1 phosphatases in cytokinesis
复制标题
中体相互作用组揭示了 PP1 磷酸酶在胞质分裂中新的意想不到的作用
DOI：
10.1101/569459
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发表时间：
2019
期刊：
影响因子：
--
通讯作者：
Capalbo L
中科院分区：
文献类型：
--
作者：
Capalbo L
中体是一个细胞器，在有丝分裂结束时，在两个子细胞之间的细胞间桥上组装。它控制子细胞的最终分离，并参与细胞命运、极性、组织组织、纤毛和管腔的形成。在这里，我们报告了复杂的中间体蛋白质-蛋白质相互作用网络（interactome）的特征，该网络识别了许多以前未知的相互作用，并为解剖中间体的多种作用提供了极有价值的资源。对该相互作用组的初步分析表明，PP1β-MYPT1磷酸酶调节细胞分裂后期的微管动力学，并使中央纺锤蛋白复合物的激酶成分MKLP1/KIF23去磷酸化。这种去磷酸化可以拮抗极光B激酶，从而改变中央纺锤蛋白在细胞分裂后期的功能和相互作用。我们的发现扩大了PP1在有丝分裂过程中的功能，并表明激酶和抗性磷酸酶分布的时空变化精细地调节了细胞分裂蛋白的活性。
The midbody is an organelle assembled at the intercellular bridge between the two daughter cells at the end of mitosis. It controls the final separation of the daughter cells and has been involved in cell fate, polarity, tissue organization, and cilium and lumen formation. Here, we report the characterization of the intricate midbody protein-protein interaction network (interactome), which identifies many previously unknown interactions and provides an extremely valuable resource for dissecting the multiple roles of the midbody. Initial analysis of this interactome revealed that PP1β-MYPT1 phosphatase regulates microtubule dynamics in late cytokinesis and de-phosphorylates the kinesin component MKLP1/KIF23 of the centralspindlin complex. This de-phosphorylation antagonizes Aurora B kinase to modify the functions and interactions of centralspindlin in late cytokinesis. Our findings expand the repertoire of PP1 functions during mitosis and indicate that spatiotemporal changes in the distribution of kinases and counteracting phosphatases finely tune the activity of cytokinesis proteins.