Why the study?
Recent advances in Cryo-EM have revealed new insights into the 10S myosin II inactivation, unfolding mechanisms, and disease associations beyond earlier TEM findings.
Cryo-EM provides high-resolution structural insights into the 10S myosin II state, which may help elucidate the mechanisms of disease-causing mutations in cardiomyopathies.
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Should not change practice; leaves open Cryo-EM studies of 10S myosin regulation in cardiovascular disease.
The compact smooth muscle 10S myosin II is a type of a monomer with folded tail and the heads bending back to interact with each other. This inactivated form is associated with regulatory and enzymatic activities affecting myosin processivity with actin filaments as well as ATPase activity. Phosphorylation by RLC can however, shuttle myosin from the inhibited 10S state to an activated 6S state, dictating the equilibrium. Multiple studies contributed by TEM have provided insights in the structural understanding of the 10S form. However, it is only recently that the true potential of Cryo-EM in deciphering the intramolecular interactions of 10S myosin state has been realized. This has led to an influx of new revelations on the 10S inactivation, unfolding mechanism and association in various diseases. This study reviews the gradual development in the structural interpretation of 10S species from TEM to Cryo-EM era. Furthermore, we discuss the utility of Cryo-EM in future myosin 10S studies and its contribution to human health.
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Bharda et al. (2022) studied this question.
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