Cruz Lissette A, Vedula Pavan, Gutierrez Natasha, Shah Neel, Rodriguez Steven, Ayee Brian, Davis Justin, Rodriguez Alexis J
Department of Biological Sciences, Rutgers University Newark, Newark, New Jersey.
Cytoskeleton (Hoboken). 2015 Dec;72(12):597-608. doi: 10.1002/cm.21265. Epub 2015 Dec 22.
Regulating adherens junction complex assembly/disassembly is critical to maintaining epithelial homeostasis in healthy epithelial tissues. Consequently, adherens junction structure and function is often perturbed in clinically advanced tumors of epithelial origin. Some of the most studied factors driving adherens junction complex perturbation in epithelial cancers are transcriptional and epigenetic down-regulation of E-cadherin expression. However, numerous reports demonstrate that post-translational regulatory mechanisms such as endocytosis also regulate early phases of epithelial-mesenchymal transition and metastatic progression. In already assembled healthy epithelia, E-cadherin endocytosis recycles cadherin-catenin complexes to regulate the number of mature adherens junctions found at cell-cell contact sites. However, following de novo epithelial cell-cell contact, endocytosis negatively regulates adherens junction assembly by removing E-cadherin from the cell surface. By contrast, following de novo epithelial cell-cell contact, spatially localized β-actin translation drives cytoskeletal remodeling and consequently E-cadherin clustering at cell-cell contact sites and therefore positively regulates adherens junction assembly. In this report we demonstrate that dynamin-mediated endocytosis and β-actin translation-dependent cadherin-catenin complex anchoring oppose each other following epithelial cell-cell contact. Consequently, the final extent of adherens junction assembly depends on which of these processes is dominant following epithelial cell-cell contact. We expressed β-actin transcripts impaired in their ability to properly localize monomer synthesis (Δ3'UTR) in MDCK cells to perturb actin filament remodeling and anchoring, and demonstrate the resulting defect in adherens junction structure and function is rescued by inhibiting dynamin mediated endocytosis. Therefore, we demonstrate balancing spatially regulated β-actin translation and dynamin-mediated endocytosis regulates epithelial monolayer structure and barrier function.
调节黏附连接复合体的组装/拆卸对于维持健康上皮组织中的上皮稳态至关重要。因此,黏附连接的结构和功能在上皮来源的临床晚期肿瘤中常常受到干扰。上皮癌中驱动黏附连接复合体紊乱的一些研究最多的因素是E-钙黏蛋白表达的转录和表观遗传下调。然而,大量报告表明,诸如内吞作用等翻译后调控机制也调节上皮-间质转化和转移进展的早期阶段。在已经组装好的健康上皮细胞中,E-钙黏蛋白内吞作用回收钙黏蛋白-连环蛋白复合体,以调节在细胞-细胞接触位点发现的成熟黏附连接的数量。然而,在新生上皮细胞-细胞接触后,内吞作用通过从细胞表面去除E-钙黏蛋白来负向调节黏附连接的组装。相比之下,在新生上皮细胞-细胞接触后,空间定位的β-肌动蛋白翻译驱动细胞骨架重塑,从而导致E-钙黏蛋白在细胞-细胞接触位点聚集,因此正向调节黏附连接的组装。在本报告中,我们证明了在上皮细胞-细胞接触后,发动蛋白介导的内吞作用和β-肌动蛋白翻译依赖性钙黏蛋白-连环蛋白复合体锚定相互对抗。因此,黏附连接组装的最终程度取决于上皮细胞-细胞接触后这些过程中的哪一个占主导地位。我们在MDCK细胞中表达了在正确定位单体合成能力上受损的β-肌动蛋白转录本(Δ3'UTR),以扰乱肌动蛋白丝的重塑和锚定,并证明通过抑制发动蛋白介导的内吞作用可以挽救由此产生的黏附连接结构和功能缺陷。因此,我们证明平衡空间调节的β-肌动蛋白翻译和发动蛋白介导的内吞作用可调节上皮单层结构和屏障功能。