Key result
CaATP slows actomyosin dissociation ~3-fold versus MgATP, prolonging strong binding and promoting futile strokes.
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Investigates CaATP's effect on actomyosin interactions, suggesting implications for muscle rigidity.
Calcium plays an essential role in muscle contraction, regulating actomyosin interaction by binding troponin of thin filaments. There are several buffers for calcium in muscle, and those buffers play a crucial role in the formation of the transient calcium wave in sarcomere upon muscle activation. One such calcium buffer in muscle is ATP. ATP is a fuel molecule, and the important role of MgATP in muscle is to bind myosin and supply energy for the power stroke. Myosin is not a specific ATPase, and CaATP also supports myosin ATPase activity. The concentration of CaATP in sarcomeres reaches 1% of all ATP available. Since 294 myosin molecules form a thick filament, naïve estimation gives three heads per filament with CaATP bound, instead of MgATP. We found that CaATP dissociates actomyosin slower than MgATP, thus increasing the time of the strong actomyosin binding. The rate of the basal CaATPase is faster than that of MgATPase, myosin readily produces futile stroke with CaATP. When calcium is upregulated, as in malignant hyperthermia, kinetics of myosin and actomyosin interaction with CaATP suggest that myosin CaATPase activity may contribute to observed muscle rigidity and enhanced muscle thermogenesis.
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Ge et al. (2019) studied Muscle Contraction / Malignant Hyperthermia. CaATP vs. MgATP was evaluated on Maximum rate of ATP-induced actomyosin dissociation (s-1). CaATP dissociates actomyosin roughly three times slower than MgATP (173.6 vs 543.9 s-1), increasing the time of strong actomyosin binding and promoting futile myosin strokes.
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