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J Cell Biol. 1982 January 1; 92(1): 79–91.
PMCID: PMC2112008

Action of cytochalasin D on cytoskeletal networks


Extraction of SC-1 cells (African green monkey kidney) with the detergent Triton X-100 in combination with stereo high-voltage electron microscopy of whole mount preparations has been used as an approach to determine the mode of action of cytochalasin D on cells. The cytoskeleton of extracted BSC-1 cells consists of substrate-associated filament bundles (stress fibers) and a highly cross-linked network of four major filament types extending throughout the cell body; 10-nm filaments, actin microfilaments, microtubules, and 2- to 3-nm filaments. Actin filaments and 2- to 3-nm filaments form numerous end- to-side contacts with other cytoskeletal filaments. Cytochalasin D treatment severely disrupts network organization, increases the number of actin filament ends, and leads to the formation of filamentous aggregates or foci composed mainly of actin filaments. Metabolic inhibitors prevent filament redistribution, foci formation, and cell arborization, but not disorganization of the three-dimensional filament network. In cells first extracted and then treated with cytochalasin D, network organization is disrupted, and the number of free filament ends is increased. Supernates of preparations treated in this way contain both short actin filaments and network fragments (i.e., actin filaments in end-to-side contact with other actin filaments). It is proposed that the dramatic effects of cytochalasin D on cells result from both a direct interaction of the drug with the actin filament component of cytoskeletal networks and a secondary cellular response. The former leads to an immediate disruption of the ordered cytoskeletal network that appears to involve breaking of actin filaments, rather than inhibition of actin filament-filament interactions (i.e., disruption of end-to-side contacts). The latter engages network fragments in an energy-dependent (contractile) event that leads to the formation of filament foci.

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Selected References

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  • Ben-Ze'ev A, Duerr A, Solomon F, Penman S. The outer boundary of the cytoskeleton: a lamina derived from plasma membrane proteins. Cell. 1979 Aug;17(4):859–865. [PubMed]
  • Bershadsky AD, Gelfand VI, Svitkina TM, Tint IS. Destruction of microfilament bundles in mouse embryo fibroblasts treated with inhibitors of energy metabolism. Exp Cell Res. 1980 Jun;127(2):421–429. [PubMed]
  • Bradford MM. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem. 1976 May 7;72:248–254. [PubMed]
  • Brenner SL, Korn ED. The effects of cytochalasins on actin polymerization and actin ATPase provide insights into the mechanism of polymerization. J Biol Chem. 1980 Feb 10;255(3):841–844. [PubMed]
  • Britch M, Allen TD. The effects of cytochalasin B on the cytoplasmic contractile network revealed by whole-cell transmission electron microscopy. Exp Cell Res. 1981 Jan;131(1):161–172. [PubMed]
  • Brown SS, Spudich JA. Cytochalasin inhibits the rate of elongation of actin filament fragments. J Cell Biol. 1979 Dec;83(3):657–662. [PMC free article] [PubMed]
  • Brown SS, Spudich JA. Mechanism of action of cytochalasin: evidence that it binds to actin filament ends. J Cell Biol. 1981 Mar;88(3):487–491. [PMC free article] [PubMed]
  • Brown S, Levinson W, Spudich JA. Cytoskeletal elements of chick embryo fibroblasts revealed by detergent extraction. J Supramol Struct. 1976;5(2):119–130. [PubMed]
  • Carter SB. Effects of cytochalasins on mammalian cells. Nature. 1967 Jan 21;213(5073):261–264. [PubMed]
  • Flanagan MD, Lin S. Cytochalasins block actin filament elongation by binding to high affinity sites associated with F-actin. J Biol Chem. 1980 Feb 10;255(3):835–838. [PubMed]
  • Godman GC, Miranda AF. Cellular contractility and the visible effects of cytochalasin. Front Biol. 1978;46:277–429. [PubMed]
  • Godman G, Woda B, Kolberg R, Berl S. Redistribution of contractile and cytoskeletal components induced by cytochalasin. I. In Hmf cells, a nontransformed fibroblastoid line. Eur J Cell Biol. 1980 Oct;22(2):733–744. [PubMed]
  • Godman G, Woda B, Kolberg R, Berl S. Redistribution of contractile and cytoskeletal components induced by cytochalasin. II. In HeLa and HEp2 cells. Eur J Cell Biol. 1980 Oct;22(2):745–754. [PubMed]
  • Griffith LM, Pollard TD. Evidence for actin filament-microtubule interaction mediated by microtubule-associated proteins. J Cell Biol. 1978 Sep;78(3):958–965. [PMC free article] [PubMed]
  • Hartwig JH, Stossel TP. Interactions of actin, myosin, and an actin-binding protein of rabbit pulmonary macrophages. III. Effects of cytochalasin B. J Cell Biol. 1976 Oct;71(1):295–303. [PMC free article] [PubMed]
  • Hartwig JH, Stossel TP. Cytochalasin B and the structure of actin gels. J Mol Biol. 1979 Nov 5;134(3):539–553. [PubMed]
  • Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. [PubMed]
  • Lenk R, Ransom L, Kaufmann Y, Penman S. A cytoskeletal structure with associated polyribosomes obtained from HeLa cells. Cell. 1977 Jan;10(1):67–78. [PubMed]
  • Lin DC, Tobin KD, Grumet M, Lin S. Cytochalasins inhibit nuclei-induced actin polymerization by blocking filament elongation. J Cell Biol. 1980 Feb;84(2):455–460. [PMC free article] [PubMed]
  • MacLean-Fletcher S, Pollard TD. Mechanism of action of cytochalasin B on actin. Cell. 1980 Jun;20(2):329–341. [PubMed]
  • Maruyama K, Hartwig JH, Stossel TP. Cytochalasin B and the structure of actin gels. II. Further evidence for the splitting of F-actin by cytochalasin B. Biochim Biophys Acta. 1980 Dec 16;626(2):494–500. [PubMed]
  • Miranda AF, Godman GC, Deitch AD, Tanenbaum SW. Action of cytochalasin D on cells of established lines. I. Early events. J Cell Biol. 1974 May;61(2):481–500. [PMC free article] [PubMed]
  • Miranda AF, Godman GC, Tanenbaum SW. Action of cytochalasin D on cells of established lines. II. Cortex and microfilaments. J Cell Biol. 1974 Aug;62(2):406–423. [PMC free article] [PubMed]
  • Osborn M, Weber K. The detertent-resistant cytoskeleton of tissue culture cells includes the nucleus and the microfilament bundles. Exp Cell Res. 1977 May;106(2):339–349. [PubMed]
  • Pollard TD. The role of actin in the temperature-dependent gelation and contraction of extracts of Acanthamoeba. J Cell Biol. 1976 Mar;68(3):579–601. [PMC free article] [PubMed]
  • Schliwa M. Proteins associated with cytoplasmic actin. Cell. 1981 Sep;25(3):587–590. [PubMed]
  • Schliwa M, van Blerkom J. Structural interaction of cytoskeletal components. J Cell Biol. 1981 Jul;90(1):222–235. [PMC free article] [PubMed]
  • Selden LA, Gershman LC, Estes JE. A proposed mechanism of action of cytochalasin D on muscle actin. Biochem Biophys Res Commun. 1980 Aug 29;95(4):1854–1860. [PubMed]
  • Tannenbaum J, Tanenbaum SW, Godman GC. The binding sites of cytochalasin D. II. Their relationship to hexose transport and to cytochalasin B. J Cell Physiol. 1977 May;91(2):239–248. [PubMed]
  • Weber K, Rathke PC, Osborn M, Franke WW. Distribution of actin and tubulin in cells and in glycerinated cell models after treatment with cytochalasin B (CB). Exp Cell Res. 1976 Oct 15;102(2):285–297. [PubMed]
  • Webster RE, Henderson D, Osborn M, Weber K. Three-dimensional electron microscopical visualization of the cytoskeleton of animal cells: immunoferritin identification of actin- and tubulin-containing structures. Proc Natl Acad Sci U S A. 1978 Nov;75(11):5511–5515. [PubMed]
  • Weihing RR. Cytochalasin B inhibits actin-related gelation of HeLa cell extracts. J Cell Biol. 1976 Oct;71(1):303–307. [PMC free article] [PubMed]
  • Wessells NK, Spooner BS, Ash JF, Bradley MO, Luduena MA, Taylor EL, Wrenn JT, Yamada K. Microfilaments in cellular and developmental processes. Science. 1971 Jan 15;171(3967):135–143. [PubMed]
  • Wolosewick JJ, Porter KR. Microtrabecular lattice of the cytoplasmic ground substance. Artifact or reality. J Cell Biol. 1979 Jul;82(1):114–139. [PMC free article] [PubMed]

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