The Drosophila membrane receptor Toll can function to promote cellular adhesion.

The product of the Toll gene is a membrane protein required for the formation of dorso-ventral polarity during early embryogenesis in Drosophila melanogaster. It acts together with the other dorsal group gene products to specify a nuclear gradient of dorsal morphogen in the syncytial blastoderm stage embryo. Here we report the presence in Toll protein of additional sequences held in common with the human membrane receptor platelet glycoprotein 1b (Gp1b). We propose that these sequences in Toll form disulphide linked extracellular domains that are important for the binding of ligands in the perivitelline space of the embryo. In addition, we show that expression of Toll protein induced in a non-adhesive cell line promotes cellular adhesion, a property held in common with the related Drosophila glycoprotein chaoptin. Toll protein in such aggregates accumulates at sites of cell-cell interaction, a characteristic displayed by other cellular adhesion molecules. Taken together these findings suggest that the biochemical function of Toll protein is more closely analogous to that of Gp1b than previously thought.