title: What can myosin VI do in cells?
abstract: The recently solved structure of the myosin VI motor demonstrates that the unique insert at the end of the motor is responsible for the reversal of the normal myosin directionality. A second class-specific insert near the nucleotide-binding pocket contributes to myosin VI's unique kinetic tuning, allowing it to function either as an actin-based transporter or as an anchoring protein. Recent biochemical and biophysical studies have shown that the native molecule can form dimers upon clustering, and cell biological studies have demonstrated that it clearly does play both transport and anchoring roles in cells. These mechanistic insights allow us to speculate on how unusual aspects of myosin VI structure and function allow it to fill unique niches in cells.
authors.affiliation: Department of Physiology University of Pennsylvania School of Medicine, 3700 Hamilton Walk, Philadelphia, PA 19104-6085 USA. Lsweeney@mail.med.upenn.edu
authors.forename: H Lee
authors.initials: HL
authors.lastname: Sweeney
authors.forename: Anne
authors.initials: A
authors.lastname: Houdusse
mesh_terms: D008841:Actin Cytoskeleton / Q000502:physiology*; D000818:Animals; D019281:Dimerization; D004331:Drosophila melanogaster / Q000502:physiology; D004705:Endocytosis / Q000502:physiology; D008958:Models, Molecular; D018995:Myosin Heavy Chains / Q000737:chemistry / Q000502:physiology*; D024701:Myosin Type V / Q000737:chemistry / Q000502:physiology; D011485:Protein Binding; D011487:Protein Conformation
chemical_list: C089785:myosin VI; D024701:Myosin Type V; D018995:Myosin Heavy Chains