Abstract
The provocative hypothesis that myosin in resting smooth muscle is in a soluble form and assembles into filaments only at the time of contraction1,2 has been disproved with the demonstration of regular arrays of myosin filaments in a variety of smooth muscles, including those shown to have been relaxed before and during fixation3–7. Nevertheless, following the observations of Suzuki et al8. on the effect of light-chain phos-phorylation on smooth muscle myosin assembly in vitro, this hypothesis has been revived with the speculation that relaxed smooth muscle contains non-phosphorylated, non-filamentous myosin that assembles into filaments only after the muscles are stimulated and myosin is phosphorylated9. Here we have used rapid freezing techniques to avoid concerns about the possible effects of fixation on the in vivo form of myosin10 and demonstrate the existence of a myosin filament lattice in relaxed vascular smooth muscles in which we also show myosin light chain phosphorylation to be minimal (<5%).
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Somlyo, A., Butler, T., Bond, M. et al. Myosin filaments have non-phosphorylated light chains in relaxed smooth muscle. Nature 294, 567–569 (1981). https://doi.org/10.1038/294567a0
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DOI: https://doi.org/10.1038/294567a0
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