| Title: | Calcineurin-mediated Dephosphorylation of Acetyl-coA Carboxylase is Required for Pheromone Biosynthesis Activating Neuropeptide (PBAN)-induced Sex Pheromone Biosynthesis in Helicoverpa armigera |
| Author(s): | Du M; Liu X; Ma N; Liu X; Wei J; Yin X; Zhou S; Rafaeli A; Song Q; An S; |
| Address: | "From the double daggerState key Laboratory of Wheat and Maize Crop Science/College of Plant Protection, Henan Agricultural University, Zhengzhou, P.R. China. section signInstitute of Plant Stress Biology, School of Life Sciences, Henan University, China. paragraph signAgricultural Research Organization, Volcani Center, Israel. ||Division of Plant Sciences, University of Missouri, Columbia, Missouri. From the double daggerState key Laboratory of Wheat and Maize Crop Science/College of Plant Protection, Henan Agricultural University, Zhengzhou, P.R. China; anshiheng@aliyun.com" |
| ISSN/ISBN: | 1535-9484 (Electronic) 1535-9476 (Print) 1535-9476 (Linking) |
| Abstract: | "Chemical signaling plays a critical role in the behavior and physiology of many animals. Female insects, as many other animals, release sex pheromones to attract males for mating. The evolutionary and ecological success of insects therefore hinges on their ability to precisely mediate (including initiation and termination) pheromone biosynthesis. Pheromone biosynthesis activating neuropeptide (PBAN) acts directly on pheromone glands to regulate sex pheromone production using Ca(2+) and cyclic-AMP as secondary messengers in the majority of species. However, the molecular mechanism downstream of the secondary messengers has not yet been elucidated in heliothine species. The present study shows that calcineurin, protein kinase A (PKA) and acetyl-coA carboxylase (ACC) are key components involved in PBAN-induced sex pheromone biosynthesis in Helicoverpa armigera using PBAN-dependent phosphoproteomics in combination with transcriptomics. RNAi-mediated knockdown and inhibitor assay demonstrated that calcineurin A is required for PBAN-induced ACC activation and sex pheromone production. Calcineurin-dependent phosphoproteomics and in vitro calcineurin phosphorylation assay further revealed that calcineurin regulated ACC activity by dephosphorylating ser84 and ser92. In addition, PKA-dependent phosphoproteomics and activity analysis revealed that PKA reduces the activity of AMP-activated protein kinase (AMPK), a negative regulator of ACC by phosphorylating the conserved ser92. Taken together, our findings indicate that calcineurin acts as the downstream signal of PBAN/G-protein receptor/Ca(2+) to activate ACC through dephosphorylation while inactivating AMPK via PKA to reduce ACC phosphorylation, thus facilitating calcineurin activation of ACC" |
| Keywords: | Acetyl-CoA Carboxylase/chemistry/genetics/*metabolism Animals Calcineurin/*metabolism Cyclic AMP-Dependent Protein Kinases/metabolism Female Gene Expression Profiling/*methods Insect Proteins/genetics/metabolism Moths/genetics/*metabolism Neuropeptides/*m; |
| Notes: | "MedlineDu, Mengfang Liu, Xiaoguang Ma, Nana Liu, Xiaoming Wei, Jizheng Yin, Xinming Zhou, Shutang Rafaeli, Ada Song, Qisheng An, Shiheng eng 2017/10/06 Mol Cell Proteomics. 2017 Dec; 16(12):2138-2152. doi: 10.1074/mcp.RA117.000065. Epub 2017 Oct 4" |
