钙黏蛋白和连环蛋白的结构与生物化学。
Structure and biochemistry of cadherins and catenins.
机构信息
Department of Biochemistry and Molecular Biophysics and Edward S. Harkness Eye Institute, Columbia University, New York, New York 10032, USA.
出版信息
Cold Spring Harb Perspect Biol. 2009 Sep;1(3):a003053. doi: 10.1101/cshperspect.a003053.
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.
经典钙黏蛋白介导细胞间黏附连接点的特异黏附。相邻细胞间钙黏蛋白胞外区的相互作用介导细胞-细胞的接触，而细胞内区域则将钙黏蛋白功能连接到下面的细胞骨架。结构、生物物理和生物化学的研究为经典钙黏蛋白介导细胞-细胞黏附的机制和特异性，以及其与细胞骨架的相互作用提供了重要的见解。通过相邻细胞间的第一个细胞外钙黏蛋白域（EC1）之间的β链交换，产生了黏附结合。这种“链交换”结合模式在经典钙黏蛋白和桥粒钙黏蛋白中是常见的，但序列比对表明其他钙黏蛋白将以不同的方式结合。经典钙黏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-连环蛋白似乎不是将β-连环蛋白稳定地桥接到肌动蛋白上，而是积极调节钙黏蛋白细胞-细胞连接处的肌动蛋白细胞骨架。
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