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Published 24 May 2004. doi:10.1083/jcb.200308141
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 165, Number 4, 539-551
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Article

 Affixin interacts with {alpha}-actinin and mediates integrin signaling for reorganization of F-actin induced by initial cell–substrate interaction

Satoshi Yamaji1, Atsushi Suzuki2, Heiwa Kanamori1, Wataru Mishima1, Ryusuke Yoshimi1, Hirotaka Takasaki1, Maki Takabayashi1, Katsumichi Fujimaki1, Shin Fujisawa1, Shigeo Ohno2, and Yoshiaki Ishigatsubo1

1 The First Department of Internal Medicine, Yokohama City University School of Medicine, Yokohama 236-0004, Japan
2 Department of Molecular Biology, Yokohama City University School of Medicine, Yokohama 236-0004, Japan

Address correspondence to Yoshiaki Ishigatsubo, The First Dept. of Internal Medicine, Yokohama City University School of Medicine, 3-9 Fuku-ura, Kanazawa-ku, Yokohama 236-0004, Japan. Tel.: (81) 45-787-2630. Fax: (81) 45-786-3444. email: ishigats{at}med.yokohama-cu.ac.jp

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 {alpha}-actinin in an ILK kinase activity–dependent manner, suggesting that integrin–ILK signaling evoked by substrate adhesion induces affixin–{alpha}-actinin interaction. The overexpression of a peptide corresponding to the {alpha}-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 {alpha}-actinin and thereby mediates integrin signaling to {alpha}-actinin, which has been shown to play a critical role in actin polymerization at focal adhesions.

Key Words: affixin; ILK; {alpha}-actinin; zyxin; Mena

The online version of this article includes supplemental material.

Abbreviations used in this paper: ABD, actin-binding domain; CH, calponin homology; DIC, differential interference contrast; FA, focal adhesion; FN, fibronectin; ILK, integrin-linked kinase; siRNA, small interference RNA; SF, stress fiber.


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