Pro-Tumorigenic Phosphorylation of p120 Catenin in Renal and Breast Cancer
Fig 5
Phosphorylation at Y228 but not at T916 is critical for the transforming ability of p120.
Breast cancer MDA-MB-231 cells were depleted of endogenous p120 and were transfected with: (A) vector control, full-length wild-type murine p120 isoform 1A (mp120-1A), or murine p120 isoform 1A where eight Src-targeted tyrosine phosphorylation sites, including Y228, were mutated to phenylalanine (mp120-8F); (B) vector control, murine wild type p120 (mp120-T916), or with murine p120 constructs where the T916 site was mutated to either alanine (mp120-T916A) or to glutamic acid (mp120-T916E). Cells in all cases were grown to soft agar and colonies were counted (mean ±SEM, n = 6; **p<0.01, *p<0.05, one-way ANOVA compared to vector control; n.s, non-significant). The western blots indicate expression of p120 using the 15D2 antibody in each case; Actin is the loading control.
