The extracellular architecture of adherens junctions revealed by crystal structures of type I cadherins.
The extracellular architecture of adherens junctions revealed by crystal structures of type I cadherins.
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DOI：
10.1016/j.str.2010.11.016
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发表时间：
2011-02-09
期刊：
影响因子：
5.7
通讯作者：
Honig, Barry
中科院分区：
文献类型：
--
作者：
Harrison, Oliver J.;Jin, Xiangshu;Hong, Soonjin;Bahna, Fabiana;Ahlsen, Goran;Brasch, Julia;Wu, Yinghao;Vendome, Jeremie;Felsovalyi, Klara;Hampton, Cheri M.;Troyanovsky, Regina B.;Ben-Shau, Avinoam;Frank, Joachim;Troyanovsky, Sergey M.;Shapiro, Lawrence;Honig, Barry
在细胞间粘附中起核心作用的粘附连接包括I型经典钙粘蛋白的簇，所述I型经典钙粘蛋白通过从相对的细胞表面延伸的细胞外结构域结合。我们发现，在晶体结构的E-和N-钙粘蛋白胞外域在这里报告，并在C-钙粘蛋白结构中看到的分子层对应于粘附连接的细胞外结构。在所有三种胞外域晶体中，钙粘蛋白通过反式粘附界面二聚化，并通过第二个顺式界面连接。由包被在脂质体上的E-钙粘蛋白胞外域形成的组装体似乎也采用这种结构。在培养细胞中野生型和突变型E-钙粘蛋白形成的连接点的荧光成像证实了来自结构证据的结论。干扰反式界面消融粘附的突变，而顺式界面突变破坏稳定的连接形成。我们的观察结果是一致的连接组件涉及强反式和弱顺式相互作用定位在胞外域的模型。
Adherens junctions, which play a central role in intercellular adhesion, comprise clusters of type I classical cadherins that bind via extracellular domains extended from opposing cell surfaces. We show that a molecular layer seen in crystal structures of E- and N-cadherin ectodomains reported here and in the C-cadherin structure corresponds to the extracellular architecture of adherens junctions. In all three ectodomain crystals, cadherins dimerize through a trans adhesive interface and are connected by a second, cis, interface. Assemblies formed by E-cadherin ectodomains coated on liposomes also appear to adopt this structure. Fluorescent imaging of junctions formed from wild-type and mutant E-cadherins in cultured cells confirm conclusions derived from structural evidence. Mutations that interfere with the trans interface ablate adhesion, whereas cis interface mutations disrupt stable junction formation. Our observations are consistent with a model for junction assembly involving strong trans and weak cis interactions localized in the ectodomain.
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