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
中科院分区:
文献类型:
--
作者:
Kodani A;Tonthat V;Wu B;Sütterlin C
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.