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Fig. 10. Model of caveolin function in the regulation of fibronectin matrix assembly by uPAR. This figure shows that, (A) in resting cells, EGFR, uPAR and Src are found in association with caveolin. Both uPAR (via its GPI anchor) and Src (via myristylation) are assumed to partially insert into the lipid bilayer. The binding of an integrin subunit on a neighboring cell (mimicked by P25; B) to uPAR results in the activation of Src, and to the Src-dependent phosphorylation of EGFR (Y845) and caveolin. Phosphorylation of Src and EGFR are dependent on caveolin, suggesting that caveolin functions as a scaffold to facilitate interactions between uPAR, Src and EGFR. (C) Phospho-caveolin and phospho-EGFR are then trafficked to focal adhesions. The redistribution of phospho-EGFR to focal adhesions is dependent on phospho-caveolin, suggesting that phospho-caveolin functions as an accessory molecule to facilitate proper trafficking of EGFR. Activated EGFR is found in complexes with 5β1 integrin, resulting in an increase in activation state. Increased integrin activation results in an increase in assembly of the fibronectin matrix.

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