A family of secreted proteins contains homology to the cysteine-rich ligand-binding domain of frizzled receptors

AUTOR(ES)

Rattner, Amir

FONTE

The National Academy of Sciences of the USA

RESUMO

This paper describes the identification of a new family of mammalian genes that encode secreted proteins containing homology to the cysteine-rich ligand-binding domain found in the frizzled family of transmembrane receptors. The secreted frizzled-related proteins (sFRPs) are approximately 30 kDa in size, and each contains a putative signal sequence, a frizzled-like cysteine-rich domain, and a conserved hydrophilic carboxy-terminal domain. The sFRPs are not the products of differential splicing of the known frizzled genes. Glycosylphosphatidylinositol-anchored derivatives of sFRP-2 and sFRP-3 produced in transfected human embryonic kidney cells confer cell-surface binding by the Drosophila Wingless protein. These observations suggest that sFRPs may function in vivo to modulate Wnt signaling, or, alternatively, as novel ligands for as yet unidentified receptors.

Documentos Relacionados

• Evidence that the cysteine-rich domain of Drosophila Frizzled family receptors is dispensable for transducing Wingless
• A tobacco gene family for flower cell wall proteins with a proline-rich domain and a cysteine-rich domain.
• The cysteine-rich frizzled domain of Frzb-1 is required and sufficient for modulation of Wnt signaling
• Ligand-binding and heterodimerization activities of a conserved region in the ligand-binding domain of the thyroid hormone receptor.
• A cysteine-rich domain of the “mannose” receptor mediates GalNAc-4-SO4 binding