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Papers In Press, published online ahead of print March 23, 2002
Molecular Biology, Princeton University, Princeton, NJ 08544
Corresponding Author: jschwarzbauer{at}molbio.princeton.edu
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 (SYF cells) 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 (PI3)-kinase inhibitor, wortmannin. CHOa5 cells, which are dependent on exogenous FN to initiate fibril formation, also showed significant reductions in matrix when treated with inhibitors of Src and PI3-kinase. Combination of both inhibitors showed an additive inhibitory effect on assembly which was concomitant with a loss of FAK phosphorylation. Decreased binding of 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 FAK, are essential for efficient initiation of FN matrix assembly.
J. Biol. Chem, 10.1074/jbc.M200270200
Submitted on January 10, 2002
Revised on March 8, 2002
Accepted on March 21, 2002
Regulatory role for SRC and P13-Kinase in initiation of fibronectin matrix assembly
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