Protein turnover dynamics suggest a diffusion-to-capture mechanism for peri-basal body recruitment and retention of intraflagellar transport proteins.

Protein turnover dynamics suggest a diffusion-to-capture mechanism for peri-basal body recruitment and retention of intraflagellar transport proteins.
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蛋白质周转动力学表明,鞭毛内运输蛋白在基底体周围的募集和保留是一种扩散到捕获的机制。

DOI:
10.1091/mbc.e20-11-0717
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发表时间:
2021-06-01
影响因子:
3.3
通讯作者:
Wallingford JB
Wallingford JB
中科院分区:
生物学3区
文献类型:
--
作者:
Hibbard JVK;Vazquez N;Satija R;Wallingford JB

文献摘要

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鞭毛内转运(IFT)对于纤毛的构建和维持是必不可少的。IFT蛋白集中在基底体,在那里它们被认为组装成火车并结合货物进行运输。为了研究IFT募集到这个基体池的机制,我们在脊椎动物多纤毛细胞中利用光漂白后的荧光恢复技术定量了8个IFT蛋白以及其他5个基底体定位蛋白的蛋白质动力学。我们发现,IFT-A和IFT-B蛋白复合体的成员表现出与其他基础身体成分不同的周转动力学。此外,已知的IFT亚复合体表现出共同的动态,表明有共同的基础体招募和/或保留机制。最后,我们通过解聚胞质MTS来评估基底体募集的机制,这表明IFT蛋白是通过扩散-捕获机制被募集到基底体的。我们对IFT蛋白动力学的研究为IFT向基底体募集提供了新的见解,这是纤毛发生和纤毛信号传递的关键步骤。
Intraflagellar transport (IFT) is essential for construction and maintenance of cilia. IFT proteins concentrate at the basal body where they are thought to assemble into trains and bind cargoes for transport. To study the mechanisms of IFT recruitment to this peri-basal body pool, we quantified protein dynamics of eight IFT proteins, as well as five other basal body localizing proteins using fluorescence recovery after photobleaching in vertebrate multiciliated cells. We found that members of the IFT-A and IFT-B protein complexes show distinct turnover kinetics from other basal body components. Additionally, known IFT subcomplexes displayed shared dynamics, suggesting shared basal body recruitment and/or retention mechanisms. Finally, we evaluated the mechanisms of basal body recruitment by depolymerizing cytosolic MTs, which suggested that IFT proteins are recruited to basal bodies through a diffusion-to-capture mechanism. Our survey of IFT protein dynamics provides new insights into IFT recruitment to basal bodies, a crucial step in ciliogenesis and ciliary signaling.