Inositol-1,4,5-trisphosphate-binding proteins controlling the phototransduction cascade of invertebrate visual cells.

The main phototransduction cascade in invertebrate visual cells involves the turnover of phosphatidylinositol, an important biochemical mechanism common to many signal-transduction systems. Light-activated rhodopsin stimulates guanine nucleotide exchange on the Gq class of G-protein, which activates phospholipase C to hydrolyze phosphatidylinositol 4,5-bisphosphate to inositol-1,4,5-trisphosphate and diacylglycerol. Subsequently, inositol-1,4,5-trisphosphate-binding proteins continue the signal cascade. Here, we report on the first inositol-1,4,5-trisphosphate-binding proteins demonstrated in an invertebrate visual system with our investigation of the photosensitive rhabdoms of squid. We screened the ability of proteins to interact with inositol-1,4,5-trisphosphate by affinity column chromatography with an inositol-1,4,5-trisphosphate analogue. We detected an inositol-1,4,5-trisphosphate-binding affinity in phospholipase C, receptor kinase and five other proteins in the cytosolic fraction and, surprisingly, rhodopsin in the membrane fraction. A binding assay with (3)H-labelled inositol-1,4,5-trisphosphate demonstrated the inositol-1,4,5-trisphosphate affinity of each of the purified proteins. Since rhodopsin, receptor kinase and phospholipase C are involved upstream of phosphatidylinositol turnover in the signal cascade, our result suggests that phosphatidylinositol turnover is important in feedback pathways in the signalling system.