Directed actin polymerization is the driving force for epithelial cell-cell adhesion
Directed actin polymerization is the driving force for epithelial cell-cell adhesion
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DOI：
10.1016/s0092-8674(00)81559-7
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发表时间：
2000-01-21
期刊：
影响因子：
64.5
通讯作者：
Fuchs, E
中科院分区：
文献类型：
--
作者：
Vasioukhin, V;Bauer, C;Fuchs, E
我们发现上皮细胞参与钙粘蛋白介导的细胞间粘附过程，以意想不到的方式利用钙和肌动蛋白聚合。钙刺激丝状足，丝状足渗透并嵌入邻近细胞。e -钙粘蛋白复合物聚集在丝状足尖端，产生嵌入点的两排拉链。相反的细胞表面被桥粒夹住，而vinculin， zyxin， VASP和Mena通过一种需要-连环蛋白的机制被招募到粘附拉链上。肌动蛋白重组和聚合，将小点合并成一行并封闭细胞边界。在角化细胞中，α -连环蛋白缺失或VASP/Mena功能受阻，丝状足嵌入，但肌动蛋白重组/聚合被阻止，膜不能密封。综上所述，揭示了细胞间粘附的动态机制，包括钙激活的丝状伪足渗透和VASP/ mena依赖的肌动蛋白重组/聚合。
We have found that epithelial cells engage in a process of cadherin-mediated intercellular adhesion that utilizes calcium and actin polymerization in unexpected ways. Calcium stimulates filopodia, which penetrate and embed into neighboring cells. E-cadherin complexes cluster at filopodia tips, generating a two-rowed zipper of embedded puncta. Opposing cell surfaces are clamped by desmosomes, while vinculin, zyxin, VASP, and Mena are recruited to adhesion zippers by a mechanism that requires alpha-catenin. Actin reorganizes and polymerizes to merge puncta into a single row and seal cell borders. In keratinocytes either null for alpha-catenin or blocked in VASP/Mena function, filopodia embed, but actin reorganization/polymerization is prevented, and membranes cannot seal. Taken together, a dynamic mechanism for intercellular adhesion is unveiled involving calcium-activated filopodia penetration and VASP/Mena-dependent actin reorganization/polymerization.