Making the Connection: Ciliary Adhesion Complexes Anchor Basal Bodies to the Actin Cytoskeleton

Making the Connection: Ciliary Adhesion Complexes Anchor Basal Bodies to the Actin Cytoskeleton
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DOI:
10.1016/j.devcel.2013.12.003
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发表时间:
2014-01-13
期刊:
影响因子:
11.8
通讯作者:
Skourides, Paris A.
Skourides, Paris A.
中科院分区:
生物学1区
文献类型:
--
作者:
Antoniades, Ioanna;Stylianou, Panayiota;Skourides, Paris A.

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纤毛与多种发育和生理过程有关,纤毛缺陷是许多遗传条件的基础。多项证据支持肌动蛋白细胞骨架在纤毛发生和纤毛功能中的关键作用。在这里,我们展示了充分表征的粘着斑(FA)蛋白,包括 FAK、Paxillin 和 Vinculin,与多纤毛细胞的基体结合并形成与肌动蛋白细胞骨架相互作用的复合物(CA)。 FAK 下调导致纤毛发生缺陷,类似于肌动蛋白细胞骨架被破坏时观察到的缺陷,包括基体迁移、对接和间距缺陷,表明 CA 将基体与肌动蛋白细胞骨架连接起来。 FA 蛋白在纤毛发生中的重要作用使我们提出,进化上的 FA 蛋白(其中许多存在于原始有鞭毛的单细胞真核生物中)可能最初进化为在鞭毛中发挥功能,后来被选为用于细胞粘附。
Cilia have been associated with diverse developmental and physiological processes, and defects in cilia underlie a number of genetic conditions. Several lines of evidence support a critical role of the actin cytoskeleton in ciliogenesis and ciliary function. Here, we show that well-characterized focal adhesion (FA) proteins, including FAK, Paxillin, and Vinculin, associate with the basal bodies of multiciliated cells and form complexes (CAs) that interact with the actin cytoskeleton. FAK downregulation leads to ciliogenesis defects similar to those observed when the actin cytoskeleton is disrupted, including defects in basal body migration, docking, and spacing, suggesting that CAs link basal bodies to the actin cytoskeleton. The important role of FA proteins in ciliogenesis leads us to propose that evolutionarily FA proteins, many of which are found in primitive flagellated unicellular eukaryotes, may have originally evolved to perform functions at flagella and were later co-opted for use in cell adhesion.