The R-Spondin family of secreted proteins is implicated in the activation of the Wnt signaling pathway. All R-spondin members require Wnt ligands and LRP6 for activity and amplify signaling of Wnt3A, Wnt1, and Wnt7A, suggesting that R-spondin proteins are general regulators of canonical Wnt signaling.
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The R-spondin (Rspo) protein family is a recently described group of four distinct human secreted proteins. Reported activities for R-spondin proteins include essential roles in vertebrate development and their ligand-type activities overlap substantially with those of the canonical Wnt ligands in that both R-spondin and canonical Wnt signaling result in the activation of beta-catenin. The R-Spondin family of secreted proteins is implicated in the activation of the Wnt signaling pathway. Although all four R-spondin proteins activate the canonical Wnt pathway, RSpo2 and 3 are more potent than RSpo1, whereas RSpo4 is relatively inactive. All R-spondin members require Wnt ligands and LRP6 for activity and amplify signaling of Wnt3A, Wnt1, and Wnt7A, suggesting that R-spondin proteins are general regulators of canonical Wnt signaling. Like RSpo1, RSpo2-4 antagonize DKK1 activity by interfering with DKK1 mediated LRP6 and Kremen association. Analysis of R-spondin (Rspo) deletion mutants indicates that the cysteine-rich furin domains shared by R-spondin family members are sufficient and essential for the amplification of Wnt signaling and inhibition of DKK1, suggesting that Wnt amplification by R-spondin proteins may be a direct consequence of DKK1 inhibition. Together, these findings indicate that R-spondin proteins modulate the Wnt pathway by a common mechanism and suggest that coexpression with specific Wnt ligands and DKK1 may determine their biological specificity.