Armenti Stephen T, Nance Jeremy
Helen L. and Martin S. Kimmel Center for Biology and Medicine at the Skirball Institute for Biomolecular Medicine, NYU School of Medicine, 10016, New York, NY, USA.
Subcell Biochem. 2012;60:279-99. doi: 10.1007/978-94-007-4186-7_12.
Caenorhabditis elegans provides a simplified, in vivo model system in which to study adherens junctions (AJs) and their role in morphogenesis. The core AJ components-HMR-1/E-cadherin, HMP-2/β-catenin and HMP-1/α-catenin-were initially identified through genetic screens for mutants with body axis elongation defects. In early embryos, AJ proteins are found at sites of contact between blastomeres, and in epithelial cells AJ proteins localize to the multifaceted apical junction (CeAJ)-a single structure that combines the adhesive and barrier functions of vertebrate adherens and tight junctions. The apically localized polarity proteins PAR-3 and PAR-6 mediate formation and maturation of junctions, while the basolaterally localized regulator LET-413/Scribble ensures that junctions remain apically positioned. AJs promote robust adhesion between epithelial cells and provide mechanical resistance for the physical strains of morphogenesis. However, in contrast to vertebrates, C. elegans AJ proteins are not essential for general cell adhesion or for epithelial cell polarization. A combination of conserved and novel proteins localizes to the CeAJ and works together with AJ proteins to mediate adhesion.
秀丽隐杆线虫提供了一个简化的体内模型系统,用于研究黏着连接(AJs)及其在形态发生中的作用。核心AJ组件——HMR-1/E-钙黏蛋白、HMP-2/β-连环蛋白和HMP-1/α-连环蛋白——最初是通过对具有体轴伸长缺陷的突变体进行遗传筛选而鉴定出来的。在早期胚胎中,AJ蛋白存在于卵裂球之间的接触部位,在上皮细胞中,AJ蛋白定位于多面顶端连接(CeAJ)——一种单一结构,它结合了脊椎动物黏着连接和紧密连接的黏附与屏障功能。顶端定位的极性蛋白PAR-3和PAR-6介导连接的形成和成熟,而基底外侧定位的调节因子LET-413/scribble确保连接保持在顶端位置。AJs促进上皮细胞之间的牢固黏附,并为形态发生的物理应变提供机械阻力。然而,与脊椎动物不同,秀丽隐杆线虫的AJ蛋白对于一般细胞黏附或上皮细胞极化并非必不可少。一组保守和新颖的蛋白质定位于CeAJ,并与AJ蛋白共同作用以介导黏附。