Roles played by a subset of integrin signaling molecules in cadherin-based cell-cell adhesion

被引:201
作者
Yano, H
Mazaki, Y
Kurokawa, K
Hanks, SK
Matsuda, M
Sabe, H [1 ]
机构
[1] Osaka Biosci Inst, Dept Biol Mol, Osaka 5650874, Japan
[2] Osaka Univ, Dept Tumor Virol, Res Inst Microbial Dis, Suita, Osaka 5650871, Japan
[3] Vanderbilt Univ, Sch Med, Dept Cell Biol, Nashville, TN 37232 USA
[4] Kyoto Univ, Grad Sch Biostudies, Kyoto 6068502, Japan
关键词
Fak; integrin; N-cadherin; paxillin; siRNA;
D O I
10.1083/jcb.200312013
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
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.
引用
收藏
页码:283 / 295
页数:13
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