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Ecdysteroid hormones are major regulators in reproduction and development ofinsects, including larval molts and metamorphosis. The functional ecdysonereceptor is a heterodimer of ECR (NR1H1) and USP-RXR (NR2B4), which is theorthologue of vertebrate retinoid X receptors (RXR alpha, beta, gamma). Bothproteins belong to the superfamily of nuclear hormone receptors,ligand-dependent transcription factors that share two conserved domains: theDNA-binding domain (DBD) and the ligand-binding domain (LBD). In order to gainfurther insight into the evolution of metamorphosis and gene regulation byecdysone in arthropods, we performed a phylogenetic analysis of both partnersof the heterodimer ECR/USP-RXR. Overall, 38 USP-RXR and 19 ECR proteinsequences, from 33 species, have been used for this analysis. Interestingly,sequence alignments and structural comparisons reveal high divergence rates,for both ECR and USP-RXR, specifically among Diptera and Lepidoptera. The mostimpressive differences affect the ligand-binding domain of USP-RXR. Inaddition, ECR sequences show variability in other domains, namely theDNA-binding and the carboxy-terminal F domains. Our data provide the firstevidence that ECR and USP-RXR may have coevolved during holometabolous insectdiversification, leading to a functional divergence of the ecdysone receptor.These results have general implications on fundamental aspects of insectdevelopment, evolution of nuclear receptors, and the design of specificinsecticides.

Rapid divergence of the ecdysone receptor in Diptera and Lepidoptera suggests coevolution between ECR and USP-RXR