Key result
Looped nonsarcomeric myosin II unfolding rate dictates filament number and length during in vitro self-assembly.
Why the study?
The mechanism of nonsarcomeric myosin II filament self-assembly and its regulation by molecular folding is little understood.
Answers are grounded in this paper and cite their sources.
Advances molecular basis of myosin assembly; leaves open how folding regulates cellular force generation in vivo.
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.
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Cross et al. (1991) studied this question. Nonsarcomeric myosin II was evaluated on Myosin filament self-assembly. In vitro, the rate at which looped nonsarcomeric myosin II molecules unfold is a key determinant of filament number and length during self-assembly.
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