Roles played by a subset of integrin signaling molecules in cadherin-based cell-cell adhesion.
Roles played by a subset of integrin signaling molecules in cadherin-based cell-cell adhesion.
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基于钙粘着蛋白的细胞 - 细胞粘附中整合素信号分子的子集发挥作用。
DOI：
10.1083/jcb.200312013
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发表时间：
2004-07-19
影响因子：
7.8
通讯作者：
Sabe, Hisataka
中科院分区：
文献类型：
--
作者：
Yano, Hajime;Mazaki, Yuichi;Kurokawa, Kazuo;Hanks, Steven K;Matsuda, Michiyuki;Sabe, Hisataka
整合素可以与钙粘蛋白相互作用。在这里，我们研究了他们可能的关系，通过使用小干扰RNA介导的蛋白质敲低HeLa细胞。我们发现，整合素信号分子的一个子集，即Fak和桩蛋白，但不是p130 Crk相关底物或富含脯氨酸的酪氨酸激酶2，参与调节基于N-钙粘蛋白的细胞-细胞粘附的过程。发现主要需要Paxillin将Fak募集至牢固的局灶性粘连。我们的研究结果表明，至少有一些涉及Fak的信号与下调细胞外周Rac 1活性的机制有关，这似乎对运动细胞中基于N-钙粘蛋白的粘附的形成很重要。我们的分析同时举例说明了Fak在维持集体细胞迁移中的细胞-细胞粘附中的重要作用，这种迁移发生在胚胎发育和癌侵袭中。
Integrins can intercommunicate with cadherins. Here, we examined their possible relationship by use of small interfering RNA–mediated protein knockdown in HeLa cells. We found that a subset of integrin signaling molecules, namely Fak and paxillin, but not p130 Crk-associated substrate or proline-rich tyrosine kinase 2, participate in processes regulating N-cadherin–based cell–cell adhesion. Paxillin was found to be required primarily for the recruitment of Fak to robust focal adhesions. Our results suggest that at least some signals involving Fak are linked to a mechanism down-regulating Rac1 activity at the cell periphery, which appears to be important for the formation of N-cadherin–based adhesions in motile cells. Our analyses simultaneously exemplified the essential role of Fak in the maintenance of cell–cell adhesions in collective cell migration, a type of migration occurring in embryonic development and carcinoma invasion.