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Originally published In Press as doi:10.1074/jbc.M200270200 on March 23, 2002

J. Biol. Chem., Vol. 277, Issue 22, 19703-19708, May 31, 2002
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Regulatory Role for Src and Phosphatidylinositol 3-Kinase in Initiation of Fibronectin Matrix Assembly*

Iwona Wierzbicka-Patynowski and Jean E. SchwarzbauerDagger

From the Department of Molecular Biology, Princeton University, Princeton, New Jersey 08544-1014

Fibronectin (FN) matrix assembly is a tightly regulated stepwise process that is initiated by interactions between FN and cell surface integrin receptors. These interactions activate many intracellular signaling pathways that regulate processes such as cell adhesion, migration, and survival. Here we demonstrate that cells lacking Src family kinases showed reduced ability to assemble FN fibrils as detected by immunofluorescence and by analysis of detergent extracts. The amount of FN matrix was further reduced by treatment with the phosphatidylinositol 3 (PI 3-kinase) inhibitor, wortmannin. CHOalpha 5 cells, which are dependent on exogenous FN to initiate fibril formation, also showed significant reductions in matrix when treated with inhibitors of Src and PI 3-kinase. Combination of both inhibitors showed an additive inhibitory effect on assembly, which was concomitant with a loss of focal adhesion kinase phosphorylation. Decreased binding of the 70-kDa amino-terminal FN fragment at matrix assembly sites further supports a role for these kinases early during the process. We propose that these two signaling molecules, which lie downstream of integrins and focal adhesion kinase, are essential for efficient initiation of FN matrix assembly.

* This work was supported by National Institutes of Health Training Grants T32 CA09528-16 (to I. W.-P.) and R01 GM 59383 (to J. E. S.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger To whom correspondence should be addressed. Tel.: 609-258-2893; Fax: 609-258-1035; E-mail: jschwarzbauer@molbio.princeton.edu.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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