Rhodopsin (P, A, , , 480 nm) of blowfly photoreceptors R1-6 is converted by light into a thermally stable metarhodopsin (M, A, , , 565 nm). In isolated blowfly rhabdoms photoconversion of P to M affects bacterial toxin-catalyzed ADP-ribosylation of a 41-kDa protein, activates phosphorylation of opsin and induces the binding of a 48-kDa phosphoprotein to the rhabdomeric membrane.ADP-ribosylation of the 41-kDa protein is catalyzed by cholera toxin and is inhibited by P -+ M conversion. The 41-kDa protein might represent the a-subunit of the G-protein, proposed to be part of the phototransduction mechanism [Blumenfeld, A. et al. (1985) Proc. Nut1 Acad. Sci. USA 82, 7116-71201.P + M conversion leads to phosphorylation of opsin at multiple binding sites: up to 4 mol phosphate are bound/mol M formed. Dephosphorylation of the phosphate binding sites is induced by photoconversion of M to P. High levels of calcium (2 mM) inhibit phosphorylation of M and increase dephosphorylation of P.Protein patterns obtained by sodium dodecyl sulfate gel electrophoresis of irradiated retina membranes show an increased incorporation of label from [y3'P]ATP also into protein bands of 48 kDa, 68 kDa and 200 kDa. Binding studies reveal that in the case of the 48-kDa protein this effect is primarily due to a light-induced binding of the protein to the photoreceptor membrane. The binding of the 48-kDa phosphoprotein is reversible: after M + P conversion the protein becomes extractable by isotonic buffers. These data suggest that in rhabdomeric photoreceptors of invertebrates light-activation of rhodopsin is coupled to an enzyme cascade in a similar way as in the ciliary'photoreceptors of vertebrates, although there may be differences, e. g. in the type of G-protein which mediates between the activated state of metarhodopsin and a signal-amplifying enzyme reaction.In the ciliary photoreceptors of vertebrates it has been shown that a light-triggered enzyme cascade (transducincyclic GMP phosphodiesterase cascade) mediates between photon absorption by rhodopsin and the closing of cation channels in the photoreceptor's plasma membrane [l -71. The mechanism underlying transduction in rhabdomeric photoreceptors of invertebrates is, at the present, not as adequately understood. The first evidence for light-controlled enzyme reactions in rhabdomeric photoreceptors was obtained by studying rhodopsin phosphorylation in cephalopod photoreceptor membranes [8, 91, a light-induced reaction that has been investigated recently in more detail [lo]. Subsequent investigations suggested a transduction mechanism showing similarities to the enzyme cascade operating in vertebrate photoreceptors; squid photoreceptor membranes Correspondence to R. Paulsen, Fakultat fur Biologie, Tierphysiologie, Ruhr-Universitat Bochum, Postfach 10 21 48, D-4630 Bochum, Federal Republic of Germany Abbreviations. GTPase, guanosine triphosphatase; HBS, Hepesbuffered saline; P, rhodopsin; M, metarhodopsin; P-state membranes, >99% P; M-state membranes, 69% of P converted to M; R1-6, pe...