Sex pheromone production for most moths is regulated by pheromone biosynthesis activating neuropeptide (PBAN). In Bombyx mori, PBAN binding triggers the opening of store-operated Ca(2+) channels, suggesting the involvement of a receptor-activated phospholipase C (PLC). In this study, we found that PLC inhibitors U73122 and compound 48/80 reduced sex pheromone production and that intracellular levels of (3)H-inositol phosphate species increased following PBAN stimulation. In addition, we amplified cDNAs from pheromone glands corresponding to PLCbeta1, PLCbeta4, PLCgamma and two G protein alpha subunits, Go and Gq. In vivo RNA interference-mediated knockdown analyses revealed that BmPLCbeta1, BmGq1, and unexpectedly, BmPLCgamma, are part of the PBAN signal transduction cascade.
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