Control of vertebrate core planar cell polarity protein localization and dynamics by Prickle 2
Control of vertebrate core planar cell polarity protein localization and dynamics by Prickle 2
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DOI：
10.1242/dev.121384
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发表时间：
2015-10-01
期刊：
影响因子：
4.6
通讯作者：
Wallingford, John B.
中科院分区：
文献类型：
--
作者：
Butler, Mitchell T.;Wallingford, John B.
细胞平面极性（PCP）是动物组织中普遍存在的一种特性，对组织的形态建成和稳态维持至关重要。在大多数情况下，这种基本性质由一组高度保守的“核心PCP”蛋白控制，其包括跨膜蛋白货车Gogh样（Vangl）和Frizzled（Fzd），以及细胞质效应物Prickle（Pk）和Dishevelled（Dvl）。这些蛋白质的不对称定位被认为是其功能的核心，了解这些蛋白质的动力学是发育生物学中的一个重要挑战。在由核心PCP蛋白组织的过程中，纤毛的定向跳动是一个重要的过程，例如脊椎动物的淋巴结、气道和大脑中的纤毛。在这里，我们利用非洲爪蟾的实时成像能力，绘制渐进的不对称本地化的荧光报告Dvl1，Pk2和Vangl1在平面极化纤毛上皮。使用这个系统，我们还描述了Pk2对Vangl1在细胞皮层的不对称动力学的影响，我们定义了Pk2控制其自身定位和影响Vangl1的区域。最后，我们的数据揭示了Vangl1和Dvl1不对称性的显著解耦。这项研究推进了我们对PCP保守蛋白功能的理解，并建立了一个快速，易于处理的平台，以促进未来在脊椎动物PCP蛋白动力学的体内研究。
Planar cell polarity (PCP) is a ubiquitous property of animal tissues and is essential for morphogenesis and homeostasis. In most cases, this fundamental property is governed by a deeply conserved set of 'core PCP' proteins, which includes the transmembrane proteins Van Gogh-like (Vangl) and Frizzled (Fzd), as well as the cytoplasmic effectors Prickle (Pk) and Dishevelled (Dvl). Asymmetric localization of these proteins is thought to be central to their function, and understanding the dynamics of these proteins is an important challenge in developmental biology. Among the processes that are organized by the core PCP proteins is the directional beating of cilia, such as those in the vertebrate node, airway and brain. Here, we exploit the live imaging capabilities of Xenopus to chart the progressive asymmetric localization of fluorescent reporters of Dvl1, Pk2 and Vangl1 in a planar polarized ciliated epithelium. Using this system, we also characterize the influence of Pk2 on the asymmetric dynamics of Vangl1 at the cell cortex, and we define regions of Pk2 that control its own localization and those impacting Vangl1. Finally, our data reveal a striking uncoupling of Vangl1 and Dvl1 asymmetry. This study advances our understanding of conserved PCP protein functions and also establishes a rapid, tractable platform to facilitate future in vivo studies of vertebrate PCP protein dynamics.