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JCS ePress online publication date 2 Dec 2003
doi: 10.1242/jcs.00845

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Research Article

FAK promotes organization of fibronectin matrix and fibrillar adhesions


Dusko Ilic*, Branka Kovacic, Kohei Johkura, David D. Schlaepfer, Nenad Tomasevic, Qin Han, Jae-Beom Kim, Kyle Howerton, Clark Baumbusch, Naoko Ogiwara, Daniel N. Streblow, Jay A. Nelson, Paul Dazin, Yuji Shino, Katsunori Sasaki, and Caroline H. Damsky
* Author for correspondence (e-mail: ilic{at}itsa.ucsf.edu)

Targeted disruption of the focal adhesion kinase (FAK) gene in mice is lethal at embryonic day 8.5 (E8.5). Vascular defects in FAK-/- mice result from the inability of FAK-deficient endothelial cells to organize themselves into vascular network. We found that, although fibronectin (FN) levels were similar, its organization was less fibrillar in both FAK-/- endothelial cells and mesoderm of E8.5 FAK-/- embryos, as well as in mouse embryonic fibroblasts isolated from mutant embryos. FAK catalytic activity, proline-rich domains, and location in focal contacts were all required for proper allocation and patterning of FN matrix. Cells lacking FAK in focal adhesions fail to translocate supramolecular complexes of integrin-bound FN and focal adhesion proteins along actin filaments to form mature fibrillar adhesions. Taken together, our data suggest that proper FN allocation and organization are dependent on FAK-mediated remodeling of focal adhesions.
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