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. Author manuscript; available in PMC: 2013 Nov 1.
Published in final edited form as: Eur J Cell Biol. 2012 Jul 22;91(11-12):878–888. doi: 10.1016/j.ejcb.2012.06.003

Figure 2. FAK regulation of Src activity.

Figure 2

(A) Schematic of FAK regulation of invadosome formation in cells that form both focal adhesions and invadosomes. FAK sequesters Src and phosphotyrosine proteins at focal adhesions to limit invadopodia formation. (B) At focal adhesions, FAK enhances the formation of rosettes. Phosphoinositides and FAK recruit Tks5 and Grb2, which interact with cortactin, N-WASp, and Arp2/3 to mediate dynamic actin polymerization. FAK interacts with p130Cas to inhibit Rho signaling during rosette formation. Although FAK at focal adhesions can sequester phosphotyrosine proteins and impair invadopodia formation, overexpression of FAK can enhance the degradation activity of invadopodia on rigid ECM substrates and promote invasive migration.