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)
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)
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DOI：
10.1074/jbc.m111.250555
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发表时间：
2011-07-08
影响因子：
4.8
通讯作者：
Matsumoto, Shogo
中科院分区：
文献类型：
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作者：
Ohnishi, Atsushi;Hull, J. Joe;Matsumoto, Shogo
雌蛾为了吸引同种雄蛾而释放的物种特异性性信息素是通过脂肪酸生物合成途径在信息素腺（PG）中从头合成的。该通路受一种称为信息素生物合成激活神经肽 (PBAN) 的神经激素调节，PBAN 是一种起源于食管下神经节的 33 个氨基酸肽。在蚕蛾（Bombyx mori）中，储存性信息素（bombykol）前体脂肪酸的细胞质脂滴在 PG 细胞中积聚。 PBAN 刺激储存的脂滴三酰甘油 (TAG) 的脂肪分解，并释放用于最终修饰的前体。 PBAN 通过 PG 细胞表面 PBAN 受体发挥其生理功能，PBAN 受体是一种属于神经调节素 U 受体家族的 G 蛋白偶联受体。 PBAN 受体介导的信号通过利用 Gq 介导的磷脂酶 C 激活的典型存储操纵通道激活途径来传递（Hull, J. J.、Kajigaya, R.、Imai, K. 和 Matsumoto, S. (2007) Biosci. Biotechnol. Biochem. 71, 1993-2001 ；Hull, J. J., Lee, J. M., Kajigaya, R. 和 Matsumoto, S. (2009) J. Biol。化学。 284、31200-31213； Hull, J. J.、Lee, J. M. 和 Matsumoto, S. (2010) 昆虫分子。生物。 19, 553-566）。然而，人们对 PG 细胞中调节 TAG 脂解作用的分子成分知之甚少。在当前的研究中，我们发现 PBAN 信号传导涉及一种名为 B. mori 脂质储存液滴蛋白-1 (BmLsd1) 的昆虫 PAT 家族蛋白的磷酸化，并且 BmLsd1 在与安贝可尔生产相关的 TAG 脂肪分解中发挥重要作用。然而，与哺乳动物 PAT 家族周脂质不同，BmLsd1 激活依赖于家蚕 Ca2+/钙调蛋白依赖性蛋白激酶 II 而不是蛋白激酶 A 的磷酸化。
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.