Advanced Search
Hariton-Shalev, A., Department of Entomology, Volcani Center, Bet Dagan 50250, Israel
Shalev, M., Edith and Joseph Fischer Enzyme Inhibitors Laboratory, Schulich Faculty of Chemistry, Technion - Israel Institute of Technology, Haifa 32000, Israel
Adir, N., Schulich Faculty of Chemistry, Technion - Israel Institute of Technology, Haifa 32000, Israel
Belausov, E., Institute of Plant Sciences, Volcani Center, Bet Dagan 50250, Israel
Altstein, M., Department of Entomology, Volcani Center, Bet Dagan 50250, Israel
Background The pyrokinin/pheromone biosynthesis-activating neuropeptide (PK/PBAN) plays a major role in regulating a wide range of physiological processes in insects. The ubiquitous and multifunctional nature of the PK/PBAN peptide family raises many questions regarding the mechanisms by which these neuropeptides elicit their effects and the nature of the receptors that mediate their functions. Methods A sex pheromone gland receptor of the PK/PBAN family from Heliothis peltigera female moth and a Spodoptera littoralis larval receptor were cloned and stably expressed, and their structural models, electrostatic potentials and cellular functional properties were evaluated. Results Homology modeling indicated highly conserved amino-acid residues in appropriate structural positions as experimentally shown for class A G-protein coupled receptors. Structural differences could be proposed and electrostatic potentials of the two receptor models revealed net charge differences. Calcium mobilization assays demonstrated that both receptors were fully functional and could initiate extracellular calcium influx to start PK/PBAN signal transduction. Evaluation of the signaling response of both receptors to PBAN and diapause hormone (DH) revealed a highly sensitive, though differential response. Both receptors responded to PBAN whereas only Spl-PK/PBAN-R exhibited a high response toward DH. Conclusions The structural, electrostatic and cellular functional differences indicate that different PK/PBAN in vivo functions may be mediated by different PK/PBAN receptors and elicited by different peptide(s). General significance The results advance our understanding of the mode of action of the PK/PBAN family, and might help in exploring novel high-affinity receptor-specific antagonists that can serve as a basis for the development of new families of insect-control agents. © 2013 Elsevier B.V.
Powered by ClearMash Solutions Ltd -
Volcani treasures
About
Terms of use
Structural and functional differences between pheromonotropic and melanotropic PK/PBAN receptors
1830
Hariton-Shalev, A., Department of Entomology, Volcani Center, Bet Dagan 50250, Israel
Shalev, M., Edith and Joseph Fischer Enzyme Inhibitors Laboratory, Schulich Faculty of Chemistry, Technion - Israel Institute of Technology, Haifa 32000, Israel
Adir, N., Schulich Faculty of Chemistry, Technion - Israel Institute of Technology, Haifa 32000, Israel
Belausov, E., Institute of Plant Sciences, Volcani Center, Bet Dagan 50250, Israel
Altstein, M., Department of Entomology, Volcani Center, Bet Dagan 50250, Israel
Structural and functional differences between pheromonotropic and melanotropic PK/PBAN receptors
Background The pyrokinin/pheromone biosynthesis-activating neuropeptide (PK/PBAN) plays a major role in regulating a wide range of physiological processes in insects. The ubiquitous and multifunctional nature of the PK/PBAN peptide family raises many questions regarding the mechanisms by which these neuropeptides elicit their effects and the nature of the receptors that mediate their functions. Methods A sex pheromone gland receptor of the PK/PBAN family from Heliothis peltigera female moth and a Spodoptera littoralis larval receptor were cloned and stably expressed, and their structural models, electrostatic potentials and cellular functional properties were evaluated. Results Homology modeling indicated highly conserved amino-acid residues in appropriate structural positions as experimentally shown for class A G-protein coupled receptors. Structural differences could be proposed and electrostatic potentials of the two receptor models revealed net charge differences. Calcium mobilization assays demonstrated that both receptors were fully functional and could initiate extracellular calcium influx to start PK/PBAN signal transduction. Evaluation of the signaling response of both receptors to PBAN and diapause hormone (DH) revealed a highly sensitive, though differential response. Both receptors responded to PBAN whereas only Spl-PK/PBAN-R exhibited a high response toward DH. Conclusions The structural, electrostatic and cellular functional differences indicate that different PK/PBAN in vivo functions may be mediated by different PK/PBAN receptors and elicited by different peptide(s). General significance The results advance our understanding of the mode of action of the PK/PBAN family, and might help in exploring novel high-affinity receptor-specific antagonists that can serve as a basis for the development of new families of insect-control agents. © 2013 Elsevier B.V.
Scientific Publication
You may also be interested in