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Adenomatosis polyposis down-regulated 1 (APCDD1) is a transmembrane glycoprotein that negatively regulates Wnt/β-catenin canonical signaling by binding with Wnt ligands and receptors.We analyzed the role of APCDD1 in the Wnt5a/c-Jun non-canonical signaling pathway and demonstrated that APCDD1 can interact in vitro with Wnt5a,a classical ligand,and Ror2,a receptor of non-canonical Wnt signaling.Furthermore,we verified the binding of APCDD1 and Ror2 in primary cells of mouse skin.Moreover,APCDD1 seems to form a complex with Ror2 and Vangl2 in the cell,and complex formation can be improved by adding Wnt5a.In the presence of Wnt5a and Ror2,APCDD1 can induce the phosphorylation of c-Jun,a transcription factor of Wnt5a non-canonical signaling,and its phosphorylation level is a readout of Wnt5a signaling.Wound-healing assay shows that APCDD1 accelerates polarized cell migration during Wnt5a-induced wound closure.Therefore,it is very likely that APCDD1 regulates Wnt5a/c-Jun non-canonical signaling as co-receptor binding with both Wnt5a and Ror2.