Abstract
THE centrifugal elongation of membranes to form extended tubular structures is a widespread form of intracellular organelle movement. Tubular lysosomes1 and the endoplasmic reticulum2, for example, undergo such extension in association with micro-tubules, and this process has been mimicked in vitro by combining purified microtubules with isolated membranes and the mechano-chemical ATPase kinesin3,4. This, along with evidence that kinesin is associated with the endoplasmic reticulum5, has led to the suggestion that kinesin provides the motive force for the formation and maintenance of elongated tubulovesicular structures in cells6,7. We have addressed this hypothesis in murine macrophages, which have prominent tubular lysosomes whose form depends on the integrity of microtubules. Here we report that two antikinesin antibodies which disrupt in vitro motility will each cause centripetal collapse of the array of tubular lysosomes when scrape-loaded into macrophages. To our knowledge this provides the first in vivo evidence that kinesin is responsible for extension of tubulovesicular structures along microtubules.
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Hollenbeck, P., Swanson, J. Radial extension of macrophage tubular lysosomes supported by kinesin. Nature 346, 864–866 (1990). https://doi.org/10.1038/346864a0
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DOI: https://doi.org/10.1038/346864a0
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