Troyanovsky Sergey
Department of Internal Medicine (Dermatology), Washington University Medical School, 660 South Euclid Ave, St. Louis, MO 63110, USA.
Eur J Cell Biol. 2005 Mar;84(2-3):225-33. doi: 10.1016/j.ejcb.2004.12.009.
While the critical function of classic cadherin in cell-cell junctions is well established, the molecular mechanism of cadherin-based adhesion remains unclear. The elusive but principal part of this adhesion process is the cadherin-cadherin interaction maintaining the intercellular contacts. This interaction is believed to be weak, suggesting that the adhesive contacts are strengthened by the cytoskeleton-dependent clustering of numerous cadherin molecules. An examination of cadherin homodimers in living cells has shown, however, that cadherin adhesive interaction is surprisingly strong. This observation implies that the strength of the adhesive contacts is regulated by the processes disintegrating cadherin dimers. The molecular structure of these dimers and mechanisms potentially responsible for their dynamics in living cells are discussed in this review.
虽然经典钙黏蛋白在细胞间连接中的关键功能已得到充分证实，但基于钙黏蛋白的黏附分子机制仍不清楚。这种黏附过程难以捉摸但又至关重要的部分是维持细胞间接触的钙黏蛋白-钙黏蛋白相互作用。这种相互作用被认为较弱，这表明黏附接触是通过众多钙黏蛋白分子依赖细胞骨架的聚集而得到加强的。然而，对活细胞中钙黏蛋白同型二聚体的研究表明，钙黏蛋白的黏附相互作用出奇地强。这一观察结果意味着黏附接触的强度是由使钙黏蛋白二聚体解体的过程所调节的。本文综述了这些二聚体的分子结构以及可能导致其在活细胞中动态变化的机制。
