Gqα-linked phospholipase Cβ1 and phospholipase Cγ are essential components of the pheromone biosynthesis activating neuropeptide (PBAN) signal transduction cascade

Authors


Shogo Matsumoto, RIKEN Advanced Science Institute, 2-1 Hirosawa, Wako, Saitama 351-0198, Japan. Tel.: + 81 48 467 9520; fax: + 81 48 462 4678; e-mail: smatsu@riken.jp; J. Joe Hull. Current address: USDA-ARS Arid Land Agricultural Research Center, 21881 N. Cardon Lane, Maricopa, AZ 85138, USA. Tel.: + 1 520 316 6334; e-mail: Joe.Hull@ars.usda.gov

Abstract

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 Ca2+ 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 3H-inositol phosphate species increased following PBAN stimulation. In addition, we amplified cDNAs from pheromone glands corresponding to PLCβ1, PLCβ4, PLCγ and two G protein α subunits, Go and Gq. In vivo RNA interference-mediated knockdown analyses revealed that BmPLCβ1, BmGq1, and unexpectedly, BmPLCγ, are part of the PBAN signal transduction cascade.

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