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Cytochalasin D does not produce net depolymerization of actin filaments in HEp-2 cells

Nature volume 287, pages 637–639 (1980)Cite this article

Abstract

The altered morphology, disappearance or ‘disruption’ of actin filaments (microfilaments) in cells treated with cytochalasin1 has sometimes been attributed to depolymerization of filamentous actin (F-actin) to its globular subunit (G-actin), but attempts to confirm that mechanism have been inconclusive. Treatment of purified actin filaments with cytochalasin B (CB) decreased their viscosity2,3, consistent with depolymerization, which was not, however, revealed by electron microscopy4, although the filaments appeared abnormal5. CB also increased the ATP-ase activity of F-actin, suggesting that it had been destabilized3, while actin filaments in the acrosomal process were not depolymerized6. CB or cytochalasin D (CD) can dissolve actin gels (reviewed in ref. 7, see also refs 8 and 9) without depolymerizing their filaments. The ‘disrupted’ actin structures in CD-treated cells bound heavy meromysin10, indicating that at least some of the cellular actin was filamentous. Using a rapid assay for G- and F-actin in cell extracts, based on the inhibition of DNase I11, we have found that neither short-nor long-term exposure of HEp-2 cells to CD produce net depolymerization of actin filaments.

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Authors and Affiliations

  1. Department of Biology, Massachusetts Institute of Technology, Cambridge, Massachusetts, 02139

    Allen Morris

  2. Department of Pathology, College of Physicians and Surgeons, Columbia University, New York, New York, 10032

    Janet Tannenbaum

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  1. Allen Morris
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Morris, A., Tannenbaum, J. Cytochalasin D does not produce net depolymerization of actin filaments in HEp-2 cells. Nature 287, 637–639 (1980). https://doi.org/10.1038/287637a0

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