Gal-3 and Cav1 work in concert to generate intra-FA domains. (A) In Mgat5^−/− cells lacking the Mgat5/galectin lattice, FAs are deficient and FAK is mostly cytosolic. (B) Gal-3-dependent integrin clustering promotes integrin activation as well as ligand-induced integrin activation (Lagana et al., 2006). Under serum-free conditions, expression of the Mgat5/galectin lattice alone can induce the formation of FAs and cell spreading (i.e., ESC-Rescue cells) but not FAK stabilization in FA domains. (C) Expression of pY14Cav1 results in the formation of an ordered membrane domain (Gaus et al., 2006) that results in the stabilization within the FA of integrin, FAK, and paxillin as well as, potentially, other FA components. Src-dependent FAK phosphorylation and its stable association with FAs lead to focal disassembly and turnover (Hamadi et al., 2005) and pY14Cav1 promotes FA disassembly such as observed in Cav1 transfected MDA-435 cells (Fig. 9). However, Gal-3/pY14Cav1-mediated stabilization of FAK in FAs is not sufficient to induce FA disassembly (Fig. 7). How domain organization occurs within the FA remains speculative and the concentration of integrin and FAK within an intra-FA liquid ordered domain is hypothetical. Indeed, the temporal and spatial nature of pY14Cav1 association with FAs remains to be determined.