The presence of certain Wnt proteins activates “canonical signaling” by binding to FZD and low-density LRP5 and LRP6 coreceptors causing Dvl to attract proteins away from the β-catenin destruction complex thereby preventing β-catenin from being degraded. If not degraded, β-catenin is stabilized and translocates to the nucleus where it binds to the transcription factor TCF4 and enhances target gene expression, including cyclin D1, c-myc, c-jun, vascular endothelial growth factor (VEGF), and several others that are associated with enhanced cell growth. In the presence of DKK1, which competitively binds to LRP5/6 causing it to bind to Kremen and become inactive, GSK3β, Axin, APC, and CKIα form a β-catenin destruction complex. CKIα and GSK3β phosphorylate β-catenin causing it to be recognized by β-transducin repeat protein, ubiquitinated, and degraded by proteasomes, thereby inhibiting “canonical signaling.”