Interplay of MPP5a with Rab11 synergistically builds epithelial apical polarity and zonula adherens

Interplay of MPP5a with Rab11 synergistically builds epithelial apical polarity and zonula adherens
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MPP5a 与 Rab11 的相互作用协同构建上皮顶端极性和粘附小带

DOI:
10.1242/dev.184457
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发表时间:
2020-01
期刊:
影响因子:
4.6
通讯作者:
Jian Zou
Jian Zou
中科院分区:
生物学2区
文献类型:
--
作者:
Yumei Hao;Yao Zhou;Yinhui Yu;Mingjie Zheng;Kechao Weng;Ziqi Kou;Jiancheng Liang;Qian Zhang;Xiajing Tang;Pinglong Xu;Brian A Link;Ke Yao;Jian Zou

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由顶端极性蛋白调控的粘附连接重塑是组织形态发生的主要驱动力,但其确切机制尚不明确。在这里,我们报告说,在斑马鱼,Crumbs复杂的组件MPP 5a相互作用,与小GTTRab 11在高尔基体运输钙粘蛋白和Crumbs组件协同顶端域,从而建立顶端上皮极性和adherens连接。相反,MPP 5a募集的Par复合物不能与Rab 11相互作用,但可能组装细胞骨架以促进钙粘蛋白的胞吐。因此,MPP 5a的功能障碍诱导上皮细胞的侵入性迁移。这种粘附连接重塑模式经常在斑马鱼透镜上皮细胞和神经上皮细胞中观察到。这些数据确定了一个未被识别的MPP 5a-Rab 11复合物,并描述了其在引导上皮细胞顶端极化和粘附小带形成中的重要作用。总结:关键的顶端极性蛋白MPP 5a与小GTP酶Rab 11相互作用,以协同引导上皮细胞中的顶端极化和粘附小带形成。
ABSTRACT Adherens junction remodeling regulated by apical polarity proteins constitutes a major driving force for tissue morphogenesis, although the precise mechanism remains inconclusive. Here, we report that, in zebrafish, the Crumbs complex component MPP5a interacts with small GTPase Rab11 in Golgi to transport cadherin and Crumbs components synergistically to the apical domain, thus establishing apical epithelial polarity and adherens junctions. In contrast, Par complex recruited by MPP5a is incapable of interacting with Rab11 but might assemble cytoskeleton to facilitate cadherin exocytosis. In accordance, dysfunction of MPP5a induces an invasive migration of epithelial cells. This adherens junction remodeling pattern is frequently observed in zebrafish lens epithelial cells and neuroepithelial cells. The data identify an unrecognized MPP5a-Rab11 complex and describe its essential role in guiding apical polarization and zonula adherens formation in epithelial cells. Summary: The key apical polarity protein MPP5a interacts with small GTPase Rab11 to guide synergistically apical polarization and zonula adherens formation in epithelial cells.
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