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首页> 外文期刊>Cell Health and Cytoskeleton >N-glycosylation status of E-cadherin controls cytoskeletal dynamics through the organization of distinct β-catenin- and γ-catenin-containing AJs
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N-glycosylation status of E-cadherin controls cytoskeletal dynamics through the organization of distinct β-catenin- and γ-catenin-containing AJs

机译：E-钙粘着蛋白的N-糖基化状态通过组织不同的含β-catenin和γ-catenin的AJ来控制细胞骨架动力学

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Abstract: N-glycosylation of E-cadherin has been shown to inhibit cell–cell adhesion. Specifically, our recent studies have provided evidence that the reduction of E-cadherin N-glycosylation promoted the recruitment of stabilizing components, vinculin and serine/threonine protein phosphatase 2A (PP2A), to adherens junctions (AJs) and enhanced the association of AJs with the actin cytoskeleton. Here, we examined the details of how N-glycosylation of E-cadherin affected the molecular organization of AJs and their cytoskeletal interactions. Using the hypoglycosylated E-cadherin variant, V13, we show that V13/β-catenin complexes preferentially interacted with PP2A and with the microtubule motor protein dynein. This correlated with dephosphorylation of the microtubule-associated protein tau, suggesting that increased association of PP2A with V13-containing AJs promoted their tethering to microtubules. On the other hand, V13/γ-catenin complexes associated more with vinculin, suggesting that they mediated the interaction of AJs with the actin cytoskeleton. N-glycosylation driven changes in the molecular organization of AJs were physiologically significant because transfection of V13 into A253 cancer cells, lacking both mature AJs and tight junctions (TJs), promoted the formation of stable AJs and enhanced the function of TJs to a greater extent than wild-type E-cadherin. These studies provide the first mechanistic insights into how N-glycosylation of E-cadherin drives changes in AJ composition through the assembly of distinct β-catenin- and γ-catenin-containing scaffolds that impact the interaction with different cytoskeletal components.
机译：摘要：E-钙黏着蛋白的N-糖基化作用已显示抑制细胞间粘附。具体而言，我们最近的研究提供了证据，即E-钙粘蛋白N-糖基化的减少促进了稳定成分，新蛋白和丝氨酸/苏氨酸蛋白磷酸酶2A（PP2A）向粘附连接点（AJs）的募集，并增强了AJs与肌动蛋白细胞骨架。在这里，我们检查了E-钙粘蛋白的N-糖基化如何影响AJs的分子组织及其细胞骨架相互作用的细节。使用低糖基化的E-钙粘蛋白变体V13，我们显示V13 /β-catenin复合物优先与PP2A和微管运动蛋白达因相互作用。这与微管相关蛋白tau的去磷酸化有关，表明PP2A与含V13的AJ的缔合增加促进了它们与微管的束缚。另一方面，V13 /γ-连环蛋白复合物与纽蛋白的相关性更高，表明它们介导了AJ与肌动蛋白细胞骨架的相互作用。 N-糖基化驱动的AJs分子组织变化具有生理意义，因为将V13转染到A253癌细胞中，既缺乏成熟的AJs也没有紧密连接（TJs），促进了稳定AJs的形成并在更大程度上增强了TJs的功能比野生型E-钙粘蛋白。这些研究首次揭示了E-钙粘蛋白的N-糖基化如何通过组装不同的含β-catenin和γ-catenin的支架来影响AJ组成的变化，这些支架影响了与不同细胞骨架成分的相互作用。

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