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. Author manuscript; available in PMC: 2019 Jul 1.
Published in final edited form as: Mol Cancer Ther. 2018 Oct 23;18(1):17–27. doi: 10.1158/1535-7163.MCT-18-0328

Figure 6: A model of FAK as a regulator of Rac1 activation in SCLC.

Figure 6:

A. “Normal” conditions in SCLC with FAK constitutively activated. FAK phosphorylation at Tyr397 leads to the activation of downstream phosphorylation-dependent signaling and to changes in the conformation of FAK and/or its binding partners, which allow Rac1 activation in the focal adhesion complex. These two events result in pro-tumoral effects. B. FAK inhibition by PF-228 and FRNK overexpression. These two methods inhibit FAK phosphorylation at Tyr397, leading to the inhibition of downstream signaling and the absence of change in conformation of FAK and/or its binding partners, which prevents Rac1 activation. These two events result in anti-tumoral effects. C. FAK inhibition by FAK shRNA transduction. The physical loss of FAK induces an inhibition of FAK phosphorylation-dependent signals but allows the activation of Rac1 because of the absence of repression by FAK. The anti-tumoral effects related to the absence of FAK are counterbalanced by the pro-tumoral effects related to Rac1 activation.