scholarly journals Molecular and neural mechanisms of sex pheromone reception and processing in the silkmoth Bombyx mori

2014 ◽  
Vol 5 ◽  
Author(s):  
Takeshi Sakurai
Keyword(s):  
Sex Pheromone ◽  
Bombyx Mori ◽  
Neural Mechanisms ◽  
Pheromone Reception

scholarly journals A Single Sex Pheromone Receptor Determines Chemical Response Specificity of Sexual Behavior in the Silkmoth Bombyx mori

PLoS Genetics ◽  
2011 ◽  
Vol 7 (6) ◽  
pp. e1002115 ◽  
Author(s):  
Takeshi Sakurai ◽  
Hidefumi Mitsuno ◽  
Stephan Shuichi Haupt ◽  
Keiro Uchino ◽  
Fumio Yokohari ◽  
...  
Keyword(s):  
Sexual Behavior ◽  
Sex Pheromone ◽  
Bombyx Mori ◽  
Pheromone Receptor ◽  
Single Sex ◽  
Chemical Response ◽  
Response Specificity

Effect of tyramine and stress on sex-pheromone production in the pre- and post-mating silkworm moth, Bombyx mori

2007 ◽  
Vol 53 (12) ◽  
pp. 1242-1249 ◽  
Author(s):  
Akinori Hirashima ◽  
Hideomi Yamaji ◽  
Takaki Yoshizawa ◽  
Eiichi Kuwano ◽  
Morifusa Eto
Keyword(s):  
Sex Pheromone ◽  
Bombyx Mori ◽  
Pheromone Production ◽  
Sex Pheromone Production

Binding of the General Odorant Binding Protein of Bombyx mori BmorGOBP2 to the Moth Sex Pheromone Components

2010 ◽  
Vol 36 (12) ◽  
pp. 1293-1305 ◽  
Author(s):  
Xiaoli He ◽  
George Tzotzos ◽  
Christine Woodcock ◽  
John A. Pickett ◽  
Tony Hooper ◽  
...  
Keyword(s):  
Sex Pheromone ◽  
Bombyx Mori ◽  
Binding Protein ◽  
Odorant Binding Protein ◽  
Sex Pheromone Components ◽  
Pheromone Components ◽  
Odorant Binding

scholarly journals Biosynthesis of Bombykol, Sex Pheromone of Bombyx mori

1972 ◽  
Vol 46 (12) ◽  
pp. 645-649 ◽  
Author(s):  
Suehiro INOUE ◽  
Yasuji HAMAMURA
Keyword(s):  
Sex Pheromone ◽  
Bombyx Mori

scholarly journals Hormone Signaling Linked to Silkmoth Sex Pheromone Biosynthesis Involves Ca2+/Calmodulin-dependent Protein Kinase II-mediated Phosphorylation of the Insect PAT Family Protein Bombyx mori Lipid Storage Droplet Protein-1 (BmLsd1)

2011 ◽  
Vol 286 (27) ◽  
pp. 24101-24112 ◽  
Author(s):  
Atsushi Ohnishi ◽  
J. Joe Hull ◽  
Misato Kaji ◽  
Kana Hashimoto ◽  
Jae Min Lee ◽  
...  
Keyword(s):  
Fatty Acid ◽  
Protein Kinase ◽  
Sex Pheromone ◽  
Bombyx Mori ◽  
Lipid Storage ◽  
Pheromone Biosynthesis ◽  
Dependent Protein Kinase ◽  
Family Protein ◽  
Protein Kinase Ii ◽  
Dependent Protein

Species-specific sex pheromones released by female moths to attract conspecific male moths are synthesized de novo in the pheromone gland (PG) via the fatty acid biosynthetic pathway. This pathway is regulated by a neurohormone termed pheromone biosynthesis activating neuropeptide (PBAN), a 33-amino acid peptide that originates in the subesophageal ganglion. In the silkmoth, Bombyx mori, cytoplasmic lipid droplets, which store the sex pheromone (bombykol) precursor fatty acid, accumulate in PG cells. PBAN stimulates lipolysis of the stored lipid droplet triacylglycerols (TAGs) and releases the precursor for final modification. PBAN exerts its physiological function via the PG cell-surface PBAN receptor, a G protein-coupled receptor that belongs to the neuromedin U receptor family. The PBAN receptor-mediated signal is transmitted via a canonical store-operated channel activation pathway utilizing Gq-mediated phospholipase C activation (Hull, J. J., Kajigaya, R., Imai, K., and Matsumoto, S. (2007) Biosci. Biotechnol. Biochem. 71, 1993–2001; Hull, J. J., Lee, J. M., Kajigaya, R., and Matsumoto, S. (2009) J. Biol. Chem. 284, 31200–31213; Hull, J. J., Lee, J. M., and Matsumoto, S. (2010) Insect Mol. Biol. 19, 553–566). Little, however, is known about the molecular components regulating TAG lipolysis in PG cells. In the current study we found that PBAN signaling involves phosphorylation of an insect PAT family protein named B. mori lipid storage droplet protein-1 (BmLsd1) and that BmLsd1 plays an essential role in the TAG lipolysis associated with bombykol production. Unlike mammalian PAT family perilipins, however, BmLsd1 activation is dependent on phosphorylation by B. mori Ca2+/calmodulin-dependent protein kinase II rather than protein kinase A.

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