Scott Jeanie A, Yap Alpha S
Division of Molecular Cell Biology, Institute for Molecular Bioscience, The University of Queensland, St Lucia, Brisbane, Queensland, Australia.
J Cell Sci. 2006 Nov 15;119(Pt 22):4599-605. doi: 10.1242/jcs.03267.
To date, alpha-catenin has been best understood as an important cytoplasmic component of the classical cadherin complex responsible for cell-cell adhesion. By virtue of its capacity to bind F-actin, alpha-catenin was commonly envisaged to support cadherin function by coupling the adhesion receptor to the actin cytoskeleton. But is alpha-catenin solely the cadherin's handmaiden? A range of recent developments suggest, instead, that its biological activity is much more complex than previously appreciated. Evidence from cellular systems and model organisms demonstrates a clear, often dramatic, role for alpha-catenin in tissue organization and morphogenesis. The morphogenetic impact of alpha-catenin reflects its capacity to mediate functional cooperation between cadherins and the actin cytoskeleton, but is not confined to this. alpha-catenin has a role in regulating cell proliferation and cadherin-independent pools of alpha-catenin may contribute to its functional impact.
迄今为止，α-连环蛋白被公认为是经典钙黏蛋白复合体中负责细胞间黏附的重要细胞质成分。凭借其与丝状肌动蛋白（F-actin）结合的能力，α-连环蛋白通常被认为是通过将黏附受体与肌动蛋白细胞骨架相连来支持钙黏蛋白的功能。但α-连环蛋白仅仅是钙黏蛋白的附属品吗？相反，一系列最新进展表明，其生物学活性比之前所认识的要复杂得多。来自细胞系统和模式生物的证据表明，α-连环蛋白在组织构建和形态发生中发挥着明确且通常十分显著的作用。α-连环蛋白的形态发生影响反映了它介导钙黏蛋白与肌动蛋白细胞骨架之间功能协作的能力，但不仅限于此。α-连环蛋白在调节细胞增殖方面发挥作用，且不依赖于钙黏蛋白的α-连环蛋白池可能对其功能影响有贡献。
