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Gqα‐linked phospholipase Cβ1 and phospholipase Cγ are essential components of the pheromone biosynthesis activating neuropeptide (PBAN) signal transduction cascade
Author(s) -
Hull J. J.,
Lee J. M.,
Matsumoto S.
Publication year - 2010
Publication title -
insect molecular biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.955
H-Index - 93
eISSN - 1365-2583
pISSN - 0962-1075
DOI - 10.1111/j.1365-2583.2010.01013.x
Subject(s) - gq alpha subunit , phospholipase c , biology , signal transduction , phospholipase , microbiology and biotechnology , gene knockdown , g protein , transduction (biophysics) , neuropeptide , inositol , biochemistry , receptor , enzyme , gene
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 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.