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哺乳动物眼中Crumbs极性复合体蛋白的常见及独特定位模式。

Common and distinctive localization patterns of Crumbs polarity complex proteins in the mammalian eye.

作者信息

Kim Jin Young, Song Ji Yun, Karnam Santi, Park Jun Young, Lee Jamie J H, Kim Seonhee, Cho Seo-Hee

机构信息

Shriners Hospitals Pediatric Research Center and Department of Anatomy and Cell Biology, Temple University School of Medicine, Philadelphia, PA 19140, USA.

Shriners Hospitals Pediatric Research Center and Department of Anatomy and Cell Biology, Temple University School of Medicine, Philadelphia, PA 19140, USA.

出版信息

Gene Expr Patterns. 2015 Jan;17(1):31-7. doi: 10.1016/j.gep.2015.01.002. Epub 2015 Jan 28.

Abstract

Crumbs polarity complex proteins are essential for cellular and tissue polarity, and for adhesion of epithelial cells. In epithelial tissues deletion of any of three core proteins disrupts localization of the other proteins, indicating structural and functional interdependence among core components. Despite previous studies of function and co-localization that illustrated the properties that these proteins share, it is not known whether an individual component of the complex plays a distinct role in a unique cellular and developmental context. In order to investigate this question, we primarily used confocal imaging to determine the expression and subcellular localization of the core Crumbs polarity complex proteins during ocular development. Here we show that in developing ocular tissues core Crumbs polarity complex proteins, Crb, Pals1 and Patj, generally appear in an overlapping pattern with some exceptions. All three core complex proteins localize to the apical junction of the retinal and lens epithelia. Pals1 is also localized in the Golgi of the retinal cells and Patj localizes to the nuclei of the apically located subset of progenitor cells. These findings suggest that core Crumbs polarity complex proteins exert common and independent functions depending on cellular context.

摘要

面包屑极性复合体蛋白对于细胞和组织极性以及上皮细胞的黏附至关重要。在上皮组织中,三种核心蛋白中的任何一种缺失都会破坏其他蛋白的定位,这表明核心成分之间存在结构和功能上的相互依赖关系。尽管之前关于功能和共定位的研究阐明了这些蛋白共有的特性,但尚不清楚该复合体的单个成分在独特的细胞和发育环境中是否发挥独特作用。为了研究这个问题,我们主要利用共聚焦成像来确定眼部发育过程中核心面包屑极性复合体蛋白的表达和亚细胞定位。在此我们表明,在发育中的眼部组织中,核心面包屑极性复合体蛋白Crb、Pals1和Patj通常呈现重叠模式,但也有一些例外。所有三种核心复合体蛋白都定位于视网膜和晶状体上皮的顶端连接。Pals1也定位于视网膜细胞的高尔基体,而Patj定位于顶端祖细胞亚群的细胞核。这些发现表明,核心面包屑极性复合体蛋白根据细胞环境发挥共同和独立的功能。

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