An angiotensin converting enzyme homolog is required for volatile pheromone detection, odorant binding protein secretion and normal courtship behavior in Drosophila melanogaster.

This article focuses on the identification and characterization of ANCE-3, a Drosophila melanogaster homolog of angiotensin converting enzyme, as a critical factor required for detection of the volatile sex pheromone 11-cis vaccenyl acetate (cVA), secretion of odorant binding proteins (OBPs), and normal courtship behavior. ANCE-3 functions in the support cells of chemosensory sensillae, where it is necessary for proper secretion of OBPs such as LUSH into the sensillum lymph; mutants lacking ANCE-3 fail to secrete these OBPs and exhibit profound defects in cVA sensitivity and markedly delayed mating behavior. Rescue experiments show that expression of wild-type ance-3 cDNA in support cells restores cVA responses, OBP localization, and courtship behavior, whereas expression in olfactory neurons does not, and mating latency defects are not solely explained by loss of cVA detection or known trichoid olfactory receptors. These findings reveal that ANCE-3 plays a non-neuronal, support cell-dependent role in pheromone detection and reproductive behavior, likely through facilitating OBP secretion, and suggest additional chemosensory sites beyond the antenna contribute to mating behaviors in Drosophila.