Mosaic Eyes is a novel component of the Crumbs complex and negatively regulates photoreceptor apical size
Mosaic Eyes is a novel component of the Crumbs complex and negatively regulates photoreceptor apical size
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DOI：
10.1242/dev.02685
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发表时间：
2006-12-15
期刊：
影响因子：
4.6
通讯作者：
Jensen, Abbie M.
中科院分区：
文献类型：
--
作者：
Hsu, Ya-Chu;Willoughby, John J.;Jensen, Abbie M.
在果蝇的发育过程中，顶基细胞极性的建立是一个重要的过程，而碎屑复合体是这一过程的主要组成部分。相比之下，人们对碎屑蛋白（Crb）在脊椎动物发育中的作用知之甚少。我们发现FERM蛋白马赛克眼（Moe）是面包屑复合体的一个新的调控成分。Moe与成人眼的Ome/Crb2a和Nok （Pals1）共免疫沉淀，体外相互作用实验表明这些相互作用是直接的。ome/crb2a的Morpholino敲低反映了更多的突变。Moe和crumb蛋白在根尖共定位，这种根尖定位需要相互的蛋白功能。通过遗传镶嵌分析，我们发现moe（-）杆状光感受器的顶端结构大大扩展，这表明moe是光感受器中碎屑蛋白功能的负调节因子。我们认为Moe是胚胎中面包屑蛋白细胞表面丰度和定位的重要调节因子。
Establishment of apical-basal cell polarity has emerged as an important process during development, and the Crumbs complex is a major component of this process in Drosophila. By comparison, little is known about the role of Crumbs (Crb) proteins in vertebrate development. We show that the FERM protein Mosaic Eyes (Moe) is a novel regulatory component of the Crumbs complex. Moe co-immunoprecipitates with Ome/Crb2a and Nok (Pals1) from adult eye and in vitro interaction experiments suggest these interactions are direct. Morpholino knockdown of ome/crb2a phenocopies the moe mutations. Moe and Crumbs proteins colocalize apically and this apical localization requires reciprocal protein function. By performing genetic mosaic analyses, we show that moe(-) rod photoreceptors have greatly expanded apical structures, suggesting that Moe is a negative regulator of Crumbs protein function in photoreceptors. We propose that Moe is a crucial regulator of Crumbs protein cell-surface abundance and localization in embryos.