title: Regulation and recycling of myosin V.
abstract: Recently there has been considerable progress in our understanding of regulation for unconventional myosin-V through elucidation of the structure of its inactive conformation and the factors that affect stability of this conformation. The inactive conformation is a folded compact structure characterized by interactions between the myosin head and the C-terminal cargo binding domain. Concentrations of Ca2+ greater than 10 microM disrupt folding. The 3-D structure determined by cryoelectron tomography of 2-D arrays in one study and electron micrographs of isolated molecules reported in another reveal similar features, but suggest different F-actin affinities for the inactive conformation. This has raised the question of how inactive myosin-V is recycled to other sites for additional rounds of cargo transport.
authors.affiliation: Institute of Molecular Biophysics, Florida State University, Tallahassee, FL 32306-4380, USA. taylor@bio.fsu.edu
authors.forename: Kenneth A
authors.initials: KA
authors.lastname: Taylor
mesh_terms: D000199:Actins / Q000378:metabolism; D000818:Animals; D002118:Calcium / Q000378:metabolism; D002147:Calmodulin / Q000378:metabolism; D008958:Models, Molecular; D024701:Myosin Type V / Q000737:chemistry / Q000378:metabolism*; D011485:Protein Binding; D011487:Protein Conformation; D021381:Protein Transport; D022142:Secretory Vesicles / Q000502:physiology
chemical_list: D000199:Actins; D002147:Calmodulin; D024701:Myosin Type V; D002118:Calcium