Retinal-binding protein as a shuttle for retinal in the rhodopsin-retinochrome system of the squid visual cells.

The molluscan visual cell is characterized by having two photopigment systems, rhodopsin and retinochrome. In connection with these systems, located separately in the rhabdomal microvilli and in the nucleated cell bodies, the physiological role of retinal-binding protein (RALBP) was investigated in the squid (Todarodes pacificus) by using 3-dehydroretinal (retinal 2) as a tracer for retinal chromophore. In dark-adapted eyes, squid RALBP is combined abundantly with 11-cis-retinal. However, upon incubation with an excess of all-trans-retinal or retinol, RALBP took up great amounts of each of them, releasing its native retinoid ligands. When an all-trans-retinal-rich RALBP thus produced was incubated in the dark with metaretinochrome 2-carrying membranes, the RALBP released all-trans-retinal to the membranes to regenerate retinochrome, taking up 11-cis-retinal 2 from metaretinochrome 2. Upon further incubation of this 11-cis-retinal 2-rich RALBP with metarhodopsin-carrying membranes, the RALBP released the 11-cis-retinal 2 to the membranes to form rhodopsin 2, receiving all-trans-retinal from metarhodopsin. These findings show that squid RALBP is capable of serving as a shuttle during the recycling of retinal in the rhodopsin-retinochrome conjugate system to maintain the photoreceptive function of the visual cells.