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- W2585488001 abstract "The unconventional myosin Ic is thought to be the principal component of the motor that adjusts mechanical responsiveness during adaptation to prolonged stimuli by hair cells, the sensory receptors of the inner ear. To better understand myosin Ic's function, we introduce a theoretical description based on myosin Ic's chemomechanical cycle and consistent with recent single-molecule studies. Thermodynamic constraints imply that the nucleotide concentrations govern the dynamics of the cycle. We explicitly calculate the probabilities of myosin Ic's occupying the different states of its cycle and show their dependence on the external force, nucleotide concentrations, and availability of actin. This analysis highlights that the strongly actin-bound states of myosin Ic are dominated by the ADP state for small forces and by the ATP state for large forces. Integrating this single-molecule cycle into a simplified ensemble description, we predict that the average number of bound myosin heads is regulated by the external force and by the nucleotide concentrations. We use our description to discuss possible mechanisms for calcium to regulate a myosin ensemble with its implication for adaptation in hair cells." @default.
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- W2585488001 date "2017-02-01" @default.
- W2585488001 modified "2023-10-17" @default.
- W2585488001 title "Regulation of Elastically Coupled Myosin IC Molecules" @default.
- W2585488001 doi "https://doi.org/10.1016/j.bpj.2016.11.1454" @default.
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