Demonstrates that random attachment of myosin to structures enables ATP-dependent movement along polar actin filaments.
Does not alter clinical practice; leaves open cytoskeletal mechanisms for cardiovascular cell research.
Myosin-coated spheres from 0.6 to 120 microns in diameter move in vitro on a substratum of polar arrays of actin cables derived from the alga Nitella. The force for this movement is provided by skeletal muscle myosin since it is ATP-dependent, and N-ethylmaleimide (NEM) inactivation of the myosin blocks movement. These observations demonstrate that attachment of myosin in a random orientation to structures will enable those structures to move along polar arrays of actin filaments.
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Sheetz et al. (1983) studied this question.
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