Visual transduction in the Drosophila compound eye functions through a pathway that couples rhodopsin to phospholipase C (PLC) and the opening of transient receptor potential (TRP) channels. This cascade differs from phototransduction in mammalian rods and cones, but is remarkably similar to signaling in mammalian intrinsically photosensitive retinal ganglion cells (ipRGCs). In this review, I focus on recent advances in the fly visual system, including the discovery of a visual cycle and insights into the machinery and mechanisms involved in generating a light response in photoreceptor cells.

The Drosophila phototransduction cascade has emerged as an attractive paradigm for understanding the molecular mechanisms underlying visual transduction, as well as other G protein-coupled signaling cascades that are activated and terminated with great rapidity. A large collection of mutants affecting the fly visual cascade have been isolated, and the nature and function of many of the affected gene products have been identified. Virtually all of the proteins, including those that were initially classified as novel, are highly related to vertebrate homologs. Recently, it has become apparent that most of the proteins central to Drosophila phototransduction are coupled into a supramolecular signaling complex, signalplex, through association with a PDZ-containing scaffold protein. The characterization of this complex has led to a re-evaluation of the mechanisms underlying the activation and deactivation of the phototransduction cascade.