New research from the Gammons lab has identified Girdin-L as a key binding partner of Dishevelled, a central regulator of Wnt signalling. The study shows that Girdin-L binds directly to the PDZ domain of DVL2 and is recruited with Dishevelled to the base of primary cilia. This interaction promotes cilia disassembly and is enhanced by Wnt5a, linking Dishevelled’s PDZ domain to β-catenin-independent Wnt signalling. The findings reveal a new mechanism linking Wnt signalling to primary cilia and may help explain how disruption of these pathways contributes to human disease.