Key result
Actin-attached myosin exhibits anisotropic stiffness, with lateral stiffness ~10-fold lower than axial stiffness.
Why the study?
Defining the mechanics and energetics of myosin motor action requires knowing fundamental parameters such as single-motor stiffness, force, and the fraction of motors attached during contraction.
To define the mechanics and energetics of the myosin motor action in muscles, it is mandatory to know fundamental parameters such as the stiffness and the force of the single myosin motor, and the fraction of motors attached during contraction. These parameters can be defined in situ using sarcomere-level mechanics in single muscle fibers under the assumption that the stiffness of a myosin dimer with both motors attached (as occurs in rigor, when all motors are attached) is twice that of a single motor (as occurs in the isometric contraction). We use a mechanical/structural model to identify the constraints that underpin the stiffness of the myosin dimer with both motors attached to actin. By comparing the results of the model with the data in the literature, we conclude that the two-fold axial stiffness of the dimers with both motors attached is justified by a stiffness of the myosin motor that is anisotropic and higher along the axis of the myofilaments. A lower azimuthal stiffness of the motor plays an important role in the complex architecture of the sarcomere by allowing the motors to attach to actin filaments at different azimuthal angles relative to the thick filament.
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Caremani et al. (2022) studied this question. Mechanical and structural modeling of the myosin motor was evaluated. A structural model demonstrates that the stiffness of the actin-attached myosin motor is anisotropic, with lateral stiffness being about one order of magnitude lower than axial stiffness.
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