Fig 2: Immunohistochemical staining detected the protein level of epithelial mesenchymal transformation-related markers in colorectal cancer rats. The bars represent the mean ± SD (n = 3). A: The images of immunohistochemical (IHC) in animal samples; B: Quantification of the protein levels of focal adhesion kinase (FAK), phosphorylate-FAK (p-FAK)/FAK, snail, Fibronectin, E-cadherin, N-cadherin and special AT-rich sequence binding protein 1 detected by IHC counting the average optical density. Compared with the non-alcohol group: bP < 0.01, aP < 0.05. SATB1: Special AT-rich sequence binding protein 1; FAK: Focal adhesion kinase; p-FAK: Phosphorylate focal adhesion kinase; qRT-PCR: Quantitative real-time polymerase chain reaction; IHC: Immunohistochemical staining; AOD: Average optical density.

Fig 3: FAK staining of chondrocytes cultured in different viscoelastic hydrogels. Green represents actin staining, blue represents nucleus staining, and red represents FAK staining. Images were taken after 14 days in culture. White arrow indicates the location of FAK.

Fig 4: Focal adhesion kinase (FAK) /P38 signaling pathway mediated the effect of WJ-MSCs ECM on HUVECs. a, b, o–q Protein expression of FAK, p-FAK, P38, p-P38, c-Myc in HUVECs was determined by western blotting. Mean ± S.E.M. n = 3. c–f, r Matrigel tube formation assay images of cumulative tube length. Bar = 50 µm. Mean ± S.E.M., n = 3. g–j, s Transwell for HUVECs migration assay and quantitative analysis of migrated HUVECs numbers. Bar = 50 µm. Mean ± S.E.M., n = 3. k–n, t Immunofluorescently stained for vascular endothelial growth factor (VEGF) of HUVECs (magnification: × 200). Bar = 50 µm. Mean ± S.E.M., n = 3. PF-573228: FAK inhibitors. The P value was calculated using one-way ANOVA and independent samples t-test. *P < 0.05, **P < 0.01 versus control

Fig 5: YAP-TEAD promoted focal adhesion formation in breast cancer cell lines through inducing FAK phosphorylation. (a) Western blot revealed that compared with the YAP-S94A mutant, overexpression of the YAP-S127A mutant could promote FAK Y397 phosphorylation. (b) Verteporfin reversed YAP-S127A-induced FAK phosphorylation in MCF7 cells. MCF7-YAP-S127A was treated with verteporfin at a dose of 10 µM for 24 h before the Western blot assay was performed. DMSO was used as a negative control. (c) Knockdown of endogenous YAP expression inhibited FAK Y397 phosphorylation in MDA-MB-231 cells. (d) Verteporfin inhibited FAK phosphorylation in MDA-MB-231 cells. Cells were treated with verteporfin at a dose of 10 µM for 24 h before Western blot assays were performed. DMSO was used as a negative control. (e, f) Western blot verified the inhibition of FAK Y397 phosphorylation via defactinib in MCF7-YAP-S127A (e) and MDA-MB-231 (f) cells. Cells were exposed to defactinib at a dose of 10 µM for 8 h before Western blot assays were performed. DMSO was used as a negative control. (g, h) Treatment with defactinib (10 µM) for 8 h decreased focal adhesions, both in MCF7-YAP-S127A (g) and MDA-MB-231 (h). DMSO was used as a negative control. Paxilin (green), F-actin (stained with phalloidin, red). Nuclei (blue). Scale bar: 20 µm. (i) Transwell invasion assays showed that exposure to defactinib (10 µM) could significantly reverse YAP-S127A-induced cell invasion in MCF7 cells. DMSO was used as a negative control. The experiment was performed in triplicate. Scale bar: 100 µm. (j) Exposure to defactinib (10 µM) significantly decreased cell invasion ability in MDA-MD-231 cells. DMSO was used as a negative control. The experiment was performed in triplicate. Scale bar: 100 µm. (k) Quantification of the relative invasion ability in (i). ** p < 0.01 by ANOVA test. (l) Quantification of the relative invasion ability in (j). ** p < 0.01 by Student’s t-test