Fig 1: ß-Catenin aa575-683 (Smad7- interacting domain (SID)) functions as a dominant-negative inhibitor of endogenous ß-catenin activity.a Smad7-myc and ß-catenin-myc alone or in combination were transfected along with increasing amounts of either EYFP-ß-catenin SID or Flag ß-catenin SID and ckm luciferase construct. Empty vector (pcDNA) was used as a control. Lysates were collected at 48 h after changing to differentiation media (DM) post-transfection. Each condition was compared to the control for the three individually transfected samples to determine fold change. Each dot represents one biological replicate, which corresponds to the mean of three technical replicates. N = 3 biological replicates per condition. The error bars represent standard error of the mean (SEM). Dunnett’s multiple comparisons test in one-way analysis of variance using GraphPad Prism 8.0 was utilized to test for statistical significance. **p = 0.01, ***p = 0.001. b Total cell lysates of ectopically expressing Flag ß-catenin SID were collected at 48 and 72 h after changing to DM post-transfection. Un-transfected cells served as controls. Cell lysates were analyzed for endogenous ß-catenin, muscle markers (Ckm, Myogenin), and Flag (ß-catenin SID) by western blot analysis. An actin blot indicated protein loading of samples