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Abstract Activation of the Wnt/beta-catenin pathway crucially depends on polymerization of dishevelled 2 (DVL2) into biomolecular condensates. However, given the low affinity of known DVL2 self-interaction sites and its low cellular concentration it is unclear how polymers can form. Here, we detect oligomeric DVL2 complexes at endogenous protein levels, using a biochemical ultracentrifugation assay.
1 Introduction The canonical Wnt/β-catenin signaling pathway is a highly intricate and conserved process that plays a vital role in various developmental and physiological functions, such as embryonic development, stem cell maintenance, and tissue homeostasis (Clevers and Nusse, 2012). In embryonic development, Wnt/β-catenin pathway is crucial for tissue differentiation, cell fate determination, and organogenesis.
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