Myosin Assembly

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Self-assembly pathway of nonsarcomeric myosin II.

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...

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Myosin Assembly The Power of Multiubiquitylation

Ubiquitylation provides a means of targeting substrate proteins for degradation by the proteasome. Novel findings in C. elegans (Hoppe et al., 2004, this issue of Cell) establish that two ubiquitin-ligases team up to multiubiquitylate the myosin chaperone UNC-45, suggesting a novel link between regulated protein degradation and myosin assembly.

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Human platelet myosin. II. In vitro assembly and structure of myosin filaments

We have used electron microscopy and solubility measurements to investigate the assembly and structure of purified human platelet myosin and myosin rod into filaments. In buffers with ionic strengths of less than 0.3 M, platelet myosin forms filaments which are remarkable for their small size, being only 320 nm long and 10-11 nm wide in the center of the bare zone. The dimensions of these filam...

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ژورنال

عنوان ژورنال: Cell

سال: 2004

ISSN: 0092-8674

DOI: 10.1016/j.cell.2004.07.020