title: 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).
abstract: 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 Ca(2+)/calmodulin-dependent protein kinase II rather than protein kinase A.
authors.affiliation: RIKEN Advanced Science Institute, 2-1 Hirosawa, Wako, Saitama, 351-0198, Japan. aohnishi@riken.jp
authors.forename: Atsushi
authors.initials: A
authors.lastname: Ohnishi
authors.forename: J Joe
authors.initials: JJ
authors.lastname: Hull
authors.forename: Misato
authors.initials: M
authors.lastname: Kaji
authors.forename: Kana
authors.initials: K
authors.lastname: Hashimoto
authors.forename: Jae Min
authors.initials: JM
authors.lastname: Lee
authors.forename: Kazuhide
authors.initials: K
authors.lastname: Tsuneizumi
authors.forename: Takehiro
authors.initials: T
authors.lastname: Suzuki
authors.forename: Naoshi
authors.initials: N
authors.lastname: Dohmae
authors.forename: Shogo
authors.initials: S
authors.lastname: Matsumoto
mesh_terms: D000818:Animals; D012831:Bombyx / Q000235:genetics / Q000378:metabolism*; D054732:Calcium-Calmodulin-Dependent Protein Kinase Type 2 / Q000235:genetics / Q000378:metabolism*; D005260:Female; D019476:Insect Proteins / Q000235:genetics / Q000378:metabolism*; D008297:Male; D009479:Neuropeptides / Q000235:genetics / Q000378:metabolism; D010766:Phosphorylation / Q000502:physiology; D012724:Sex Attractants / Q000096:biosynthesis* / Q000235:genetics; D015398:Signal Transduction / Q000502:physiology*
chemical_list: D019476:Insect Proteins; D009479:Neuropeptides; D012724:Sex Attractants; C079709:pheromone biosynthesis activating neuropeptide, Helicoverpa zea; D054732:Calcium-Calmodulin-Dependent Protein Kinase Type 2