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Calmodulin Modulation of Insect Ryanodine Receptors
Lianyun Lin1, Heng Jiang1, Hadiatullah Hadiatullah1
1Tianjin Key Laboratory for Modern Drug Delivery & High-Efficiency; Collaborative Innovation Center of Chemical Science and Engineering; School of Pharmaceutical Science and Technology, Tianjin University, Tianjin300072, China.
Journal of Agricultural and Food Chemistry
|December 16, 2022
Summary
Insect calmodulin regulates insect ryanodine receptors (RyRs), crucial for pest control. Targeting the calmodulin-binding domain enhances insecticide efficacy, offering new pest management strategies.
Area of Science:
- Molecular biology
- Insect physiology
- Biochemistry
Background:
- Ryanodine receptors (RyRs) are critical calcium channels in the endoplasmic reticulum.
- Understanding RyR regulation is key for developing effective pest control strategies.
Purpose of the Study:
- To investigate the role of insect calmodulin (CaM) in regulating RyRs from diamondback moth and fall armyworm.
- To explore the potential of the CaM-RyR interaction as a target for novel insecticides.
Main Methods:
- Recombinant expression and pull-down assays of insect RyRs and CaM.
- Site-directed mutagenesis to alter the CaM-binding domain (CaMBD).
- Isothermal titration calorimetry (ITC) and mutagenesis studies to characterize binding thermodynamics and identify key residues.
Main Results:
- Insect CaM binds to insect RyR, but less efficiently than to rabbit RyR1 or modified insect RyR.
- Mutating the insect CaMBD to resemble rabbit RyR1 enhanced CaM binding.
- Enhanced CaM binding in the mutant insect RyR led to increased sensitivity to chlorantraniliprole (CHL).
Conclusions:
- The CaM-CaMBD interaction is a significant regulatory site for insect RyRs.
- This interface represents a potential target for developing insecticide synergists that act as molecular glues.
- Identifying specific residues involved in insect-specific regulation opens avenues for targeted pest control development.
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