title: Myosin-V motility: these levers were made for walking.
abstract: Myosin-Va, a processive actin-based motor thought to be involved in organelle transport, now stands ready to join myosin-II (from muscle) as one of the most highly characterized members of the myosin superfamily. Recent reports from the laboratories of Goldman and colleagues and Selvin and colleagues have provided unprecedented, high-resolution views of the structural changes that take place while this motor moves along its track. Taken together, the new results indicate that myosin-Va tilts its light chain binding domains to 'walk' along actin in a hand-over-hand fashion.
authors.affiliation: Department of Molecular, Cellular and Developmental Biology, Yale University, 342 Kline Biology Tower, 266 Whitney Avenue, New Haven, CT 06511, USA. matthew.tyska@yale.edu
authors.forename: Matthew J
authors.initials: MJ
authors.lastname: Tyska
authors.forename: Mark S
authors.initials: MS
authors.lastname: Mooseker
mesh_terms: D000818:Animals; D008958:Models, Molecular; D020409:Molecular Motor Proteins / Q000378:metabolism*; D009068:Movement; D018995:Myosin Heavy Chains / Q000378:metabolism*; D024701:Myosin Type V / Q000378:metabolism*; D011487:Protein Conformation
chemical_list: D020409:Molecular Motor Proteins; D024701:Myosin Type V; D018995:Myosin Heavy Chains