title: Self-assembly pathway of nonsarcomeric myosin II.
abstract: Cells need to control the location and timing of actomyosin-dependent force generation, and appear to do so in the first instance by regulating myosin filament self-assembly (Yumura and Fukui, 1985). The mechanism of the self-assembly is little understood. In vitro it is a true self-assembly, which requires a short domain at the C terminus of the myosin molecule. The availability of this domain appears suppressed by the folding of the molecule into a compact, looped state. In vitro, the rate at which these looped molecules unfold turns out to be a key determinant of filament number and filament length.
authors.affiliation: MRC Laboratory of Molecular Biology, Cambridge, UK.
authors.forename: R A
authors.initials: RA
authors.lastname: Cross
authors.forename: T P
authors.initials: TP
authors.lastname: Hodge
authors.forename: J
authors.initials: J
authors.lastname: Kendrick-Jones
mesh_terms: D008841:Actin Cytoskeleton / Q000378:metabolism; D000818:Animals; D002465:Cell Movement; D008871:Microvilli / Q000378:metabolism; D009130:Muscle, Smooth / Q000378:metabolism; D009218:Myosins / Q000378:metabolism*
chemical_list: D009218:Myosins