Structure and Biochemistry of Cadherins and Catenins
Structure and Biochemistry of Cadherins and Catenins
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DOI：
10.1101/cshperspect.a003053
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发表时间：
2009-09-01
影响因子：
7.2
通讯作者：
Weis, William I.
中科院分区：
文献类型：
--
作者：
Shapiro, Lawrence;Weis, William I.
经典钙粘蛋白介导细胞间粘附连接处的特异性粘附。来自贴壁细胞的钙粘蛋白胞外域之间的相互作用介导细胞-细胞接触，而胞内区域功能性地将钙粘蛋白连接到底层细胞骨架。结构，生物物理和生物化学的研究提供了重要的见解经典钙粘蛋白和它们的相互作用与细胞骨架的细胞-细胞粘附的机制和特异性。粘附结合通过来自相邻细胞的伴侣钙粘蛋白的第一胞外钙粘蛋白结构域（EC 1）之间的β链交换而产生。这种“链交换”结合模式是常见的经典和桥粒钙粘蛋白，但序列比对表明，其他钙粘蛋白将结合不同。经典钙粘蛋白的细胞内区域与p120和β-连环蛋白结合，β-连环蛋白与F-肌动蛋白结合蛋白α-连环蛋白结合。α-连环蛋白不是稳定地将β-连环蛋白桥接到肌动蛋白，而是在基于钙粘蛋白的细胞-细胞接触中主动调节肌动蛋白细胞骨架。
Classical cadherins mediate specific adhesion at intercellular adherens junctions. Interactions between cadherin ectodomains from apposed cells mediate cell-cell contact, whereas the intracellular region functionally links cadherins to the underlying cytoskeleton. Structural, biophysical, and biochemical studies have provided important insights into the mechanism and specificity of cell-cell adhesion by classical cadherins and their interplay with the cytoskeleton. Adhesive binding arises through exchange of beta strands between the first extracellular cadherin domains (EC1) of partner cadherins from adjacent cells. This "strand-swap" binding mode is common to classical and desmosomal cadherins, but sequence alignments suggest that other cadherins will bind differently. The intracellular region of classical cadherins binds to p120 and beta-catenin, and beta-catenin binds to the F-actin binding protein alpha-catenin. Rather than stably bridging beta-catenin to actin, it appears that alpha-catenin actively regulates the actin cytoskeleton at cadherin-based cell-cell contacts.