Moesin (Moe) is a key component to link the actin cytoskeleton to the plasma membrane for stable surface structures such as microvilli. Moe function depends on phosphorylation in its actin binding domain. Phosphorylated Moe (p-Moe) is an active form that binds to both actin filaments and membrane proteins to tether them together. Levels of p-Moe are regulated by a kinase, Slik, and a phosphatase, Pp1-87B, which work antagonistically. Clic (Chloride Intracellular Channel) is proposed to interact with Moe and regulate levels of p-Moe. For example, loss of Clic function results in increased levels of p-Moe in the larval salivary gland. To elucidate how Clic regulates p-Moe levels in cell types rich in actin-based surface structures, we chose the rhabdomeres of photoreceptors in the compound eyes of Drosophila melanogaster. The rhabdomeres are a cylinder like surface structure consisting of ~60,000 microvilli. As we observed in the larval salivary gland, p-Moe levels were elevated in Clic-deficient clones in the pupal retina. The rhabodomeres are extremely sensitive to levels of Moe phosphoregulators like Slik. We examined rhabodomere structures in different genetic backgrounds using transmission electron microscopy. We changed expression of Slik and Pp1-87B in a wild-type as well as Clic-deficient background. We also examined rhabdomere structures in loss-of-function as well as gain-of-function of Moe in the presence or absence of Clic. We found that Clic suppresses Slik and Pp1-87B functions. Effects of Clic on these Moe phosphoregulators also depend on the level of Moe. Clic showed more pronounced effects on Slik than Pp1-87B when less Moe was available in photoreceptors, while Pp1-87B activity was more suppressed by Clic when Moe is more abundant. Based on these findings, we propose that Clic plays a critical role in maintaining a proper level of p-Moe in photoreceptors in the compound eye.