Distribution of myosin and relationship to actin organization in cortical and subcortical areas of antibody-labelled, quick-frozen, deep-etched fibroblast cytoskeletons.

In this study I describe the ultrastructural distribution of myosin in cortical and subcortical areas of antibody-labelled, quick-frozen fibroblasts. In many cells myosin was present in small variably spaced and sized (0.23-0.39 micron long), nonaligned patches, while in other cells much larger periodically spaced patches of more uniform length (0.27 micron) were found. In all regions of the cytoskeleton myosin was found, primarily on linear bundles of actin filaments running parallel to the cell's long axis. Myosin was absent from single actin filaments, actin filaments perpendicular to actin bundles aligned with the cell's long axis, and actin filaments, such as geodome vertices and parts of the cortex, which had a complex interwoven appearance. These data indicate that in motile non-muscle cells myosin exerts force only in a unidirectional manner. Recognisable myosin filaments were never observed even in cells incubated either in N-ethylmaleimide or sodium azide. The presence of myosin in, and almost to the very edge of, the cortex suggests that the cellular control of actomyosin based movement is direct and over short-range distances. Large numbers of small cross-linking filaments were found in association with cortical and subcortical actin. Their relationship to myosin and overall actin geometry is discussed.