Key result
Biochemical characterization and electron microscopy revealed that myosin VI is a monomeric, non-processive motor with a large working stroke of 18 nm.
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Advances cellular motor insights in cardiomyocytes; leaves open its role in cardiac contractility.
Myosin VI moves towards the minus end of actin filaments unlike all the other myosins so far studied, suggesting that it has unique properties and functions. Myosin VI is present in clathrin-coated pits and vesicles, in membrane ruffles and in the Golgi complex, indicating that it has a wide variety of functions in the cell. To investigate the cellular roles of myosin VI, we have identified a variety of myosin VI-binding partners and characterized their interactions. As an alternative approach, we have studied the in vitro properties of intact myosin VI. Previous studies assumed that myosin VI existed as a dimer but our biochemical characterization and electron microscopy studies reveal that myosin VI is a monomer. Using an optical tweezers force transducer, we showed that monomeric myosin VI is a non-processive motor with a large working stroke of 18 nm. Potential roles for myosin VI in cells are discussed.
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Lister et al. (2004) studied this question. Myosin VI was evaluated on In vitro properties of intact myosin VI. Biochemical characterization and electron microscopy revealed that myosin VI is a monomeric, non-processive motor with a large working stroke of 18 nm.
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