We have recently discovered that worms sense light and engage in phototaxis behavior that is essential to their survival. Our work has led to the identification of photoreceptor neurons and molecules in the C. elegans phototransduction pathway. Through electrophysiological interrogation, we discovered that LITE-1 acts in ASJ to transduce light signals through a G protein-mediated process which requires membrane-associated guanylate cyclases. This pathway shares striking similarities to those found in some vertebrate photoreceptor cells. Interestingly,
lite-1 belongs to the invertebrate taste receptor family. Discovering that a gustatory receptor could permit light sensation in worms, we wondered if expression of other known light sensing molecules, such as opsins, could function similarly in worms. In other words, could structurally distinct, mammalian opsins, hijack the C. elegans phototransduction machinery to restore photosensory behavior in
lite-1 mutants? To this end we made transgenic worms expressing bovine rhodopsin and discovered that it can restore light sensitivity in
lite-1 mutants. These findings demonstrate that divergent photoreceptor molecules can share functional homology.