title: Myosin V from head to tail.
abstract: Myosin V (myoV), a processive cargo transporter, has arguably been the most well-studied unconventional myosin of the past decade. Considerable structural information is available for the motor domain, the IQ motifs with bound calmodulin or light chains, and the cargo-binding globular tail, all of which have been crystallized. The repertoire of adapter proteins that link myoV to a particular cargo is becoming better understood, enabling cellular transport processes to be dissected. MyoV is processive, meaning that it takes many steps on actin filaments without dissociating. Its extended lever arm results in long 36-nm steps, making it ideal for single molecule studies of processive movement. In addition, electron microscopy revealed the structure of the inactive, folded conformation of myoV when it is not transporting cargo. This review provides a background on myoV, and highlights recent discoveries that show why myoV will continue to be an active focus of investigation.
authors.affiliation: Department of Molecular Physiology and Biophysics, 149 Beaumont Avenue, University of Vermont, Burlington, Vermont 05405, USA. kathleen.trybus@uvm.edu
authors.forename: K M
authors.initials: KM
authors.lastname: Trybus
mesh_terms: D001692:Biological Transport; D008958:Models, Molecular; D024701:Myosin Type V / Q000737:chemistry* / Q000378:metabolism / Q000502:physiology; D017434:Protein Structure, Tertiary; D020691:rab GTP-Binding Proteins / Q000378:metabolism
chemical_list: D024701:Myosin Type V; D020691:rab GTP-Binding Proteins