Actin depolymerization is not involved in phototransduction

Abstract

The rhabdomeral microvilli in the eyes of invertebrates have a cytoskeletal core (Saibil, 1982; Blest et al., 1982a, b, 1983) of actin (de Couet et al., 1984; Arikawa et al., 1990; Williams, 1991; Caiman & Chamberlain, 1992) which might be involved in phototransduction. Tsukita et al. (1988) suggested that light stimulation triggers the breakdown of the microvillar actin filament complex and that this may play a role in phototransduction. To test their suggestion, we pressure-injected phalloidin into Limulus ventral photoreceptors to prevent actin depolymerization (Cooper, J.A., 1987) and tested to see if this blocked phototransduction. We have previously shown that injected rho-damine-phalloidin brightly labels the microvillar actin filaments in living Limulus ventral photoreceptors for several hours (Feng et al., 1994). In the experiments reported here, phalloidin unconjugated with fluorophore was used, and the final concentration in the cell after many small injections from a pipette containing 10 mg/ml phalloidin was estimated to be 1 mg/ml (1.2 mM). This concentration is 100 times higher than that used in an extracted cellular preparation to stabilize actin (Biegel & Pachter, 1992). Fig. 1 shows that the responses to steps of light at different intensities are normal 1 h after phalloidin injection. Similar results were obtained in two other cells.