Abstract
It has been suggested that the polymerization of actin to form actin filaments is critical for many functions in non-muscle cells including phagocytosis, cell division, secretion and cell motility1,2. In support of this suggestion, many of these functions are inhibited by cytochalasins3 which also inhibit the actin nuclei-induced polymerization of purified actin4–7. Recent studies suggest that the cytochalasins (cytochalasins B, D and E) inhibit polymerization by binding to the growing end of actin filaments and blocking the further addition of monomeric actin molecules4,7–9. If the cytochalasins inhibit cellular contractile functions by a similar mechanism, they could be useful tools in determining whether actin polymerization is required for specific processes within cells. Blood platelets provide an excellent system for testing this as exposure of platelets to thrombin results in a rapid polymerization of actin10,11. We have now studied the effects of the cytochalasins on thrombin-induced actin polymerization and report here the first clear evidence that cytochalasins inhibit actin polymerization in intact cells.
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Fox, J., Phillips, D. Inhibition of actin polymerization in blood platelets by cytochalasins. Nature 292, 650–652 (1981). https://doi.org/10.1038/292650a0
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DOI: https://doi.org/10.1038/292650a0
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