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- Title
Affixin interacts with α-actinin and mediates integrin signaling for reorganization of E-actin induced by initial cell -- substrate interaction.
- Authors
Yamaji, Satoshi; Suzuki, Atsushi; Kanamori, Heiwa; Mishima, Wataru; Yoshimi, Ryusuke; Takasaki, Hirotaka; Takabayashi, Maki; Fujimaki, Katsumichi; Fujisawa, Shin; Ohno, Shigeo; Ishigatsubo, Yoshiaki
- Abstract
The linking of integrin to cytoskeleton is a critical event for an effective cell migration. Previously, we have reported that a novel integrin-linked kinase (ILK)--binding protein, affixin, is closely involved in the linkage between integrin and cytoskeleton in combination with ILK. In the present work, we demonstrated that the second calponin homology domain of affixin directly interacts with α-actinin in an ILK kinase activity--dependent manner, suggesting that integrin-ILK signaling evoked by substrate adhesion induces affixin--α-actinin interaction. The overexpression of a peptide corresponding to the α-actinin--binding site of affixin as well as the knockdown of endogenous affixin by small interference RNA resulted in the blockade of cell spreading. Time-lapse observation revealed that in both experiments cells were round with small peripheral blebs and failed to develop lamellipodia, suggesting that the ILK--affixin complex serves as an integrin-anchoring site for α-actinin and thereby mediates integrin signaling to α-actinin, which has been shown to play a critical role in actin polymerization at focal adhesions.
- Subjects
ACTIN; INTEGRINS; CELL communication; CYTOSKELETON; CELL migration; CARRIER proteins
- Publication
Journal of Cell Biology, 2004, Vol 165, Issue 4, p539
- ISSN
0021-9525
- Publication type
Article
- DOI
10.1083/jcb.200308141