Abstract
A central question in vision research is the identity of the biochemical pathway that underlies the phototransduction process. It is now well established that cGMP is the internal messenger of visual transduction in vertebrate rods and that a guanine nucleotide-binding protein (the G-protein transducin) couples the photoexcited rhodopsin to cGMP hydrolysis (for review, see Stryer 1986). Much less is known about phototransduction in the invertebrate photoreceptors, and even the identity of the second messenger of phototransduction is still in dispute. This is because both inositol triphosphate (InsP3) (Brown et al. 1984; Fein et al. 1984) and cGMP (Johnson et al. 1986) have been found to excite the Limulus ventral photoreceptors. We have initiated combined electrophysiological and biochemical studies of phototransduction in Drosophila and Musca flies, since the extensive genetic and physiological background of Drosophila mutants can be used to assign physiological roles to biochemical reactions that unavoidably must be measured under in vitro conditions that disrupt the spatial arrangement of the photoreceptor cell.
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© 1989 Springer-Verlag Berlin Heidelberg
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Selinger, Z., Minke, B. (1989). Phosphoinositide Metabolism and Visual Signal Transduction. In: Gehring, U., Helmreich, E.J.M., Schultz, G. (eds) Molecular Mechanisms of Hormone Action. 40. Colloquium der Gesellschaft für Biologische Chemie 6.– 8. April 1989 in Mosbach/Baden, vol 40. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-75022-9_13
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DOI: https://doi.org/10.1007/978-3-642-75022-9_13
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