FEATURES

FAMILY

DESCRIPTION

Also known as TOLL_DROME, Tl. Receptor for the cleaved activated form of spz, spaetzle C-106 (PubMed:12872120). Binding to spaetzle C-106 activates the Toll signaling pathway and induces expression of the antifungal peptide drosomycin (PubMed:12872120, PubMed:8808632, PubMed:10973475). Component of the extracellular signaling pathway that establishes dorsal-ventral polarity in the embryo (PubMed:3931919). Promotes heterophilic cellular adhesion (PubMed:2124970). Involved in synaptic targeting of motoneurons RP5 and V to muscle 12 (M12); functions as a repulsive cue inhibiting motoneuron synapse formation on muscle 13 (M13) to guide RP5 and V to the neighboring M12, where its expression is repressed by tey (PubMed:20504957). May also function in embryonic neuronal survival and the synaptic targeting of SNa motoneurons (PubMed:19018662). In the absence of ligand, forms a low-affinity disulfide-linked homodimer (PubMed:24733933). In the presence of ligand, crystal structures show one Tl molecule bound to a spaetzle C-106 homodimer (PubMed:24282309, PubMed:24733933). However, the active complex probably consists of two Tl molecules bound to a spaetzle C-106 homodimer (PubMed:24282309, PubMed:24733933). This is supported by in vitro experiments which also show binding of the spaetzle C-106 dimer to 2 Tl receptors (PubMed:12872120). Ligand binding induces conformational changes in the extracellular domain of Tl (PubMed:24282309). This may enable a secondary homodimerization interface at the C-terminus of the Tl extracellular domain (PubMed:24282309).

EXTERNAL LINKS

Tl

Mutations

Mutation(s) distribution

Mutations table