摘要：SummaryDuring canonical Wnt signaling, the Wnt receptor complex is sequestered together with glycogen synthase kinase 3 (GSK3) and Axin inside late endosomes, known as multivesicular bodies (MVBs). Here, we present experiments showing that Wnt causes the endocytosis of focal adhesion (FA) proteins and depletion of Integrin β 1 (ITGβ1) from the cell surface. FAs and integrins link the cytoskeleton to the extracellular matrix. Wnt-induced endocytosis caused ITGβ1 depletion from the plasma membrane and was accompanied by striking changes in the actin cytoskeleton.In situprotease protection assays in cultured cells showed that ITGβ1 was sequestered within membrane-bounded organelles that corresponded to Wnt-induced MVBs containing GSK3 and FA-associated proteins. Anin vivomodel usingXenopusembryos dorsalized byWnt8mRNA showed that ITGβ1 depletion decreased Wnt signaling. The finding of a crosstalk between two major signaling pathways, canonical Wnt and focal adhesions, should be relevant to human cancer and cell biologyGraphical abstractDisplay OmittedHighlights•Wnt protein treatment triggers rapid endocytosis of focal adhesion components•Integrin-β1 is depleted form the cell surface by Wnt within minutes•InXenopusassays, Integrin-β1 depletion inhibits Wnt overexpression•The canonical Wnt and focal adhesion signaling pathways crosstalk via endocytosisCell biology; Developmental biology; Omics
