Extracellular signals are often transduced by dynamic protein complexes (‘signalosomes’) that are assembled by cytoplasmic hub proteins following their recruitment to agonist-bound transmembrane receptors. One example is the Wnt signalosome, which is assembled by Dishevelled following its recruitment to the Frizzled seven-transmembrane receptors upon their binding to Wnt agonists. Wnt signalosome assembly by Dishevelled depends on dynamic and reversible head-to-tail polymerization by its DIX domain (1-3). This increases the local concentration of Dishevelled rapidly and dramatically, thus boosting its avidity for low-affinity binding partners, which empowers Dishevelled to interact with signaling effectors even if these are present at low cellular concentration (4). One key effector is Axin, which assembles a multiprotein complex via polymerization of its own DIX domain (‘Axin degradasome’) to destabilize b-catenin (5), a Wnt effector with pivotal roles in normal animal development and cancer (6). Upon Wnt stimulation, Dishevelled blocks the activity of the Axin degradasome, by co-polymerizing with Axin through heterotypic DIX-DIX interactions (7). We have recently discovered that the DEP domain of Dishevelled mediates signalosome assembly, by undergoing dimerization via ‘domain swapping’. This provides cross-linking of Dishevelled polymers, which illustrates a fundamental principle underlying signalosome formation (8). Both DIX-dependent polymerization and DEP-dependent dimerization require transient local concentration of Dishevelled. This could be provided by clathrin-coated pits to which Dishevelled may be recruited via binding to the Frizzled receptor following Wnt-dependent coupling between Frizzled and the LRP6 co-receptor (which itself is thought to be pre-localised in nascent pits). We shall discuss recent evidence that supports our model of clathrin-coated pits serving as locales for Wnt signal transduction.