Key result
Cryo-electron microscopy has enabled characterization of myosin-actin interactions and myosin-2 regulation, providing increased insight into the force generation mechanism.
Why the study?
Advances in cryo-EM have enabled structural characterisation of myosin interacting with actin and its shutdown state, prompting a review of accomplishments and future therapeutic directions.
Cryo-EM advancements have significantly improved the understanding of myosin structure-function relationships, which may guide future therapeutic interventions for myosin-related diseases.
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Advances structural insights into myosin function; leaves open translation to therapies for myosin-related cardiomyopathies.
Myosins are a superfamily of ATP-driven actin-dependent molecular motors that are responsible for diverse functions from muscle contraction to cell division. The resolution revolution in cryo-EM has enabled characterisation of the interaction of myosin with its actin track in several states of the myosin motor cycle, for multiple myosin classes, allowing increased insight into the force generation mechanism. A major advancement in our understanding of myosin-2 regulation has come through solving structures of its shutdown state, dysregulation of which is implicated in multiple diseases. This review will discuss what has been accomplished so far with cryoEM, what is still yet to do, but within reach, and how better understanding of myosin structure-function relationships may lead to future therapeutic interventions.
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McMillan et al. (2022) reported a review. Cryo-electron microscopy has enabled characterization of myosin-actin interactions and myosin-2 regulation, providing increased insight into the force generation mechanism.
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