Ecdysone receptor (EcR) and its heterodimer, ultraspiracle protein (USP), are ligand dependent transcriptional factors that mediate the action of molting hormone 20-hydroxyecdysone. Both USP and EcR have been shown to be phosphoprotein and their phosphorylation is mediated by protein kinase C (PKC). Our results show that PKC regulates 20E-induced protein expression via EcR and USP phosphorylation and subcellular translocation. Using proteomic method, we have identified 14 proteins which are induced by 20E but inhibited by PKC specific inhibitor Chelerythrine Chloride(CC). These proteins were verified at both transcriptional and translational levels by real-time PCR and/or Western blot.