Par6 alpha interacts with the dynactin subunit p150 Glued and is a critical regulator of centrosomal protein recruitment.

Par6 alpha interacts with the dynactin subunit p150 Glued and is a critical regulator of centrosomal protein recruitment.
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DOI:
10.1091/mbc.e10-05-0430
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发表时间:
2010-10-01
影响因子:
3.3
通讯作者:
Sütterlin C
Sütterlin C
中科院分区:
生物学3区
文献类型:
--
作者:
Kodani A;Tonthat V;Wu B;Sütterlin C

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中心体和中心粒卫星的组成成分Par6α的缺失导致了控制微管组织的中心体蛋白的错误定位。Par6α结合动力蛋白亚单位p150Gluc并调节其定位。我们认为Par6α通过与p150Glued的结合促进中心体蛋白的转运。中心体含有控制间期和有丝分裂中微管细胞骨架组织的蛋白质。它的蛋白质组成通过选择性和细胞周期依赖的招募、保留和移除成分受到严格调控。然而,蛋白质传递到中心体的机制还不完全清楚。我们描述了极性蛋白PAR6α在蛋白质转运到中心体中的一种新功能。我们在中心体和中心粒卫星上检测到Par6α,在那里它与中心粒卫星蛋白PCm-1和动力蛋白亚单位p150Glued相互作用。PAR6α缺失导致p150葡萄糖和中心体成分的错误定位,这些成分是微管在中心体锚定的关键。因此,在缺乏PAR6α的情况下,微管细胞骨架的组织发生了严重的变化,细胞分裂受阻。我们提出了一个模型,在该模型中,Par6α通过其与动力蛋白亚单位p150Glued的联系来控制中心体组织。
Depletion of Par6α, a component of the centrosome and centriolar satellites, caused mislocalization of centrosomal proteins that control microtubule organization. Par6α bound the dynactin subunit p150Glued and regulated its localization. We propose that Par6α facilitates centrosomal protein delivery through its association with p150Glued. The centrosome contains proteins that control the organization of the microtubule cytoskeleton in interphase and mitosis. Its protein composition is tightly regulated through selective and cell cycle–dependent recruitment, retention, and removal of components. However, the mechanisms underlying protein delivery to the centrosome are not completely understood. We describe a novel function for the polarity protein Par6α in protein transport to the centrosome. We detected Par6α at the centrosome and centriolar satellites where it interacted with the centriolar satellite protein PCM-1 and the dynactin subunit p150Glued. Depletion of Par6α caused the mislocalization of p150Glued and centrosomal components that are critical for microtubule anchoring at the centrosome. As a consequence, there were severe alterations in the organization of the microtubule cytoskeleton in the absence of Par6α and cell division was blocked. We propose a model in which Par6α controls centrosome organization through its association with the dynactin subunit p150Glued.