Nuclear localization of the zebrafish tight junction protein nagie oko
Nuclear localization of the zebrafish tight junction protein nagie oko
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DOI：
10.1002/dvdy.21389
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发表时间：
2008-01-01
影响因子：
2.5
通讯作者：
Abdelilah-Seyfried, Salim
中科院分区：
文献类型：
--
作者：
Bit-Avragim, Nana;Rohr, Stefan;Abdelilah-Seyfried, Salim
紧密连接相关的 MAGUK 蛋白 nagie oko 与果蝇 Stardust、与 lin-7 1 (Pals1) 相关的小鼠蛋白和人 MAGUK p55 亚家族成员 5 (Mpp5) 密切相关。作为进化上保守的 Crumbs 蛋白复合物的组成部分，nagie oko 对于维持上皮细胞极性至关重要。在这里，我们表明 nagie oko 包含预测的核输出和两个保守的核定位信号。我们发现预测的核输出信号的丢失会导致核蛋白积累。我们发现 nagie oko 核输入受到两个核定位信号和进化保守区域 1 (ECR1) 的冗余控制，该区域将 nagie oko 与 Par6-aPKC 连接起来。最后，缺乏核输入和输出信号的 nagie oko 缺失形式补充了细胞极性和上皮完整性方面的几种 nagie oko 突变体缺陷。这一发现为了解这种重要的细胞极性调节剂的潜在新颖和未知作用提供了一个切入点。
The tight junctions-associated MAGUK protein nagie oko is closely related to Drosophila Stardust, mouse protein associated with lin-seven 1 (Pals1), and human MAGUK p55 subfamily member 5 (Mpp5). As a component of the evolutionarily conserved Crumbs protein complex, nagie oko is essential for the maintenance of epithelial cell polarity. Here, we show that nagie oko contains a predicted nuclear export and two conserved nuclear localization signals. We find that loss of the predicted nuclear export signal results in nuclear protein accumulation. We show that nagie oko nuclear import is redundantly controlled by the two nuclear localization signals and the evolutionarily conserved region 1 (ECR1), which links nagie oko with Par6-aPKC. Finally, deletion forms of nagie oko that lack nuclear import and export signals complement several nagie oko mutant defects in cell polarity and epithelial integrity. This finding provides an entry point to potentially novel and unknown roles of this important cell polarity regulator.