Involvement of a Go-type G-protein coupled to guanylate cyclase in the phototransduction cGMP cascade of molluscan simple photoreceptors.

Simple photoreceptors, namely photoresponsive neurons, designated as A-P-1, Es-1, Ip-2 and Ip-1, exist in the sea slug Onchidium ganglion. Previous works has shown that, of these, Ip-2 and Ip-1 respond to light with a hyperpolarizing receptor potential, caused by the opening of light-dependent, cGMP-gated K+ channels, whereas A-P-1 and Es-1 are depolarized by light, owing to the closing of the same K+ channels. The present study of Ip-2 or Ip-1 cells was undertaken to identify the G-proteins that couple light to the activation of guanylate cyclase (GC), thereby leading to the opening of K+ channels and the consequent hyperpolarizing photocurrents. The specific channel blocker, 4-aminopyridine (4-AP), and a GC inhibitor, LY-83583, both suppressed this hyperpolarizing photocurrent. N-ethylmaleimide and GDP-beta-S also inhibited this photocurrent, consistent with the involvement of G-proteins. Mastoparan an activator of both Go- and Gi-type G-proteins, induced an outward current. Furthermore, benzalkonium chloride (C(16)BAC), a selective activator of Go, dose-dependently generated an outward current similar to that induced by mastoparan. Both of these outward currents were susceptible to 4-AP, LY-83583 and N-ethylmaleimide. Taken together, these results suggest that phototransduction in Ip-2 or Ip-1 cells is triggered by a Go-type G-protein coupled to GC. Thus, this new cGMP cascade contrasts with the conventional phototransduction cGMP cascade mediated by the Gt-type G-protein coupled to phosphodiesterase, seen in the vertebrate photoreceptors and the above A-P-1 or Es-1 cells.