Dvl LLPS induces Axin recruitment and signalosome formation upon Wnt ligand binding to promote Wnt/β-catenin signaling. In the absence of Wnt-ligand signaling, Dvl2 forms polymerized condensates via the IDR1 (denoted as number 1 in the Dvl structure) and DIX domains, while the β-catenin DC phosphorylates and degrades β-catenin. Following stimulation with Wnt3a ligand, Dvl2 is recruited to the Fzd receptor at the PM and reduces Axin-DC condensate organization stability and function to degrade β-catenin. Following stable Dvl2 recruitment at the PM, the Dvl2 IDR1 region with the DIX domain recruits the Axin complex to the PM, resulting in complete destabilization of APC and β-catenin from the DC, forming the signalosome. The resulting unphosphorylated β-catenin translocates to the nucleus to induce canonical Wnt target gene expression. Figure created with BioRender.com.