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. 1987 Oct 1;105(4):1473–1478. doi: 10.1083/jcb.105.4.1473

Effects of cytochalasin and phalloidin on actin

PMCID: PMC2114638  PMID: 3312229

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Selected References

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  1. Barden J. A., Miki M., Hambly B. D., Dos Remedios C. G. Localization of the phalloidin and nucleotide-binding sites on actin. Eur J Biochem. 1987 Feb 2;162(3):583–588. doi: 10.1111/j.1432-1033.1987.tb10679.x. [DOI] [PubMed] [Google Scholar]
  2. Bonder E. M., Fishkind D. J., Mooseker M. S. Direct measurement of critical concentrations and assembly rate constants at the two ends of an actin filament. Cell. 1983 Sep;34(2):491–501. doi: 10.1016/0092-8674(83)90382-3. [DOI] [PubMed] [Google Scholar]
  3. Bonder E. M., Mooseker M. S. Cytochalasin B slows but does not prevent monomer addition at the barbed end of the actin filament. J Cell Biol. 1986 Jan;102(1):282–288. doi: 10.1083/jcb.102.1.282. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Bonder E. M., Mooseker M. S. Direct electron microscopic visualization of barbed end capping and filament cutting by intestinal microvillar 95-kdalton protein (villin): a new actin assembly assay using the Limulus acrosomal process. J Cell Biol. 1983 Apr;96(4):1097–1107. doi: 10.1083/jcb.96.4.1097. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Bray D., Thomas C. Unpolymerized actin in fibroblasts and brain. J Mol Biol. 1976 Aug 25;105(4):527–544. doi: 10.1016/0022-2836(76)90233-3. [DOI] [PubMed] [Google Scholar]
  6. Brenner S. L., Korn E. D. Stimulation of actin ATPase activity by cytochalasins provides evidence for a new species of monomeric actin. J Biol Chem. 1981 Aug 25;256(16):8663–8670. [PubMed] [Google Scholar]
  7. Brown S. S., Spudich J. A. Cytochalasin inhibits the rate of elongation of actin filament fragments. J Cell Biol. 1979 Dec;83(3):657–662. doi: 10.1083/jcb.83.3.657. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Brown S. S., Spudich J. A. Mechanism of action of cytochalasin: evidence that it binds to actin filament ends. J Cell Biol. 1981 Mar;88(3):487–491. doi: 10.1083/jcb.88.3.487. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Carlier M. F., Criquet P., Pantaloni D., Korn E. D. Interaction of cytochalasin D with actin filaments in the presence of ADP and ATP. J Biol Chem. 1986 Feb 15;261(5):2041–2050. [PubMed] [Google Scholar]
  10. Casella J. F., Flanagan M. D., Lin S. Cytochalasin D inhibits actin polymerization and induces depolymerization of actin filaments formed during platelet shape change. Nature. 1981 Sep 24;293(5830):302–305. doi: 10.1038/293302a0. [DOI] [PubMed] [Google Scholar]
  11. Coluccio L. M., Tilney L. G. Phalloidin enhances actin assembly by preventing monomer dissociation. J Cell Biol. 1984 Aug;99(2):529–535. doi: 10.1083/jcb.99.2.529. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Cooper J. A., Bryan J., Schwab B., 3rd, Frieden C., Loftus D. J., Elson E. L. Microinjection of gelsolin into living cells. J Cell Biol. 1987 Mar;104(3):491–501. doi: 10.1083/jcb.104.3.491. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Coué M., Korn E. D. Interaction of plasma gelsolin with G-actin and F-actin in the presence and absence of calcium ions. J Biol Chem. 1985 Dec 5;260(28):15033–15041. [PubMed] [Google Scholar]
  14. Dancker P., Löw I. Complex influence of cytochalasin B on actin polymerization. Z Naturforsch C. 1979 Aug;34(7-8):555–557. doi: 10.1515/znc-1979-7-811. [DOI] [PubMed] [Google Scholar]
  15. Dancker P., Löw I., Hasselbach W., Wieland T. Interaction of actin with phalloidin: polymerization and stabilization of F-actin. Biochim Biophys Acta. 1975 Aug 19;400(2):407–414. doi: 10.1016/0005-2795(75)90196-8. [DOI] [PubMed] [Google Scholar]
  16. Detmers P. A., Goodenough U. W., Condeelis J. Elongation of the fertilization tubule in Chlamydomonas: new observations on the core microfilaments and the effect of transient intracellular signals on their structural integrity. J Cell Biol. 1983 Aug;97(2):522–532. doi: 10.1083/jcb.97.2.522. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Estes J. E., Selden L. A., Gershman L. C. Mechanism of action of phalloidin on the polymerization of muscle actin. Biochemistry. 1981 Feb 17;20(4):708–712. doi: 10.1021/bi00507a006. [DOI] [PubMed] [Google Scholar]
  18. Faulstich H., Schäfer A. J., Weckauf M. The dissociation of the phalloidin-actin complex. Hoppe Seylers Z Physiol Chem. 1977 Feb;358(2):181–184. doi: 10.1515/bchm2.1977.358.1.181. [DOI] [PubMed] [Google Scholar]
  19. Flanagan M. D., 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] [Google Scholar]
  20. Fox J. E., Phillips D. R. Inhibition of actin polymerization in blood platelets by cytochalasins. Nature. 1981 Aug 13;292(5824):650–652. doi: 10.1038/292650a0. [DOI] [PubMed] [Google Scholar]
  21. Frieden C., Patane K. Differences in G-actin containing bound ATP or ADP: the Mg2+-induced conformational change requires ATP. Biochemistry. 1985 Jul 16;24(15):4192–4196. doi: 10.1021/bi00336a056. [DOI] [PubMed] [Google Scholar]
  22. Füchtbauer A., Jockusch B. M., Maruta H., Kilimann M. W., Isenberg G. Disruption of microfilament organization after injection of F-actin capping proteins into living tissue culture cells. 1983 Jul 28-Aug 3Nature. 304(5924):361–364. doi: 10.1038/304361a0. [DOI] [PubMed] [Google Scholar]
  23. Gabbiani G., Montesano R., Tuchweber B., Salas M., Orci L. Phalloidin-induced hyperplasia of actin filaments in rat hepatocytes. Lab Invest. 1975 Nov;33(5):562–569. [PubMed] [Google Scholar]
  24. Goddette D. W., Frieden C. Actin polymerization. The mechanism of action of cytochalasin D. J Biol Chem. 1986 Dec 5;261(34):15974–15980. [PubMed] [Google Scholar]
  25. Goddette D. W., Frieden C. The binding of cytochalasin D to monomeric actin. Biochem Biophys Res Commun. 1985 May 16;128(3):1087–1092. doi: 10.1016/0006-291x(85)91051-4. [DOI] [PubMed] [Google Scholar]
  26. Goddette D. W., Frieden C. The kinetics of cytochalasin D binding to monomeric actin. J Biol Chem. 1986 Dec 5;261(34):15970–15973. [PubMed] [Google Scholar]
  27. Goddette D. W., Uberbacher E. C., Bunick G. J., Frieden C. Formation of actin dimers as studied by small angle neutron scattering. J Biol Chem. 1986 Feb 25;261(6):2605–2609. [PubMed] [Google Scholar]
  28. Godman G. C., Miranda A. F. Cellular contractility and the visible effects of cytochalasin. Front Biol. 1978;46:277–429. [PubMed] [Google Scholar]
  29. Harris H. E., Weeds A. G. Plasma gelsolin caps and severs actin filaments. FEBS Lett. 1984 Nov 19;177(2):184–188. doi: 10.1016/0014-5793(84)81280-6. [DOI] [PubMed] [Google Scholar]
  30. Hartwig J. H., Stossel T. P. Cytochalasin B and the structure of actin gels. J Mol Biol. 1979 Nov 5;134(3):539–553. doi: 10.1016/0022-2836(79)90366-8. [DOI] [PubMed] [Google Scholar]
  31. Howard T. H., Oresajo C. O. The kinetics of chemotactic peptide-induced change in F-actin content, F-actin distribution, and the shape of neutrophils. J Cell Biol. 1985 Sep;101(3):1078–1085. doi: 10.1083/jcb.101.3.1078. [DOI] [PMC free article] [PubMed] [Google Scholar]
  32. Kirschner M. W. Implications of treadmilling for the stability and polarity of actin and tubulin polymers in vivo. J Cell Biol. 1980 Jul;86(1):330–334. doi: 10.1083/jcb.86.1.330. [DOI] [PMC free article] [PubMed] [Google Scholar]
  33. Lal A. A., Korn E. D. Reinvestigation of the inhibition of actin polymerization by profilin. J Biol Chem. 1985 Aug 25;260(18):10132–10138. [PubMed] [Google Scholar]
  34. Lutz F., Glossmann H., Frimmer M. Binding of 3 H-desmethylphalloin to isolated plasma membranes from rat liver. Naunyn Schmiedebergs Arch Pharmacol. 1972;273(4):341–351. doi: 10.1007/BF00499668. [DOI] [PubMed] [Google Scholar]
  35. Löw I., Dancker P. Effect of cytochalasin B on formation and properties of muscle F-actin. Biochim Biophys Acta. 1976 May 14;430(2):366–374. doi: 10.1016/0005-2728(76)90092-x. [DOI] [PubMed] [Google Scholar]
  36. MacLean-Fletcher S., Pollard T. D. Mechanism of action of cytochalasin B on actin. Cell. 1980 Jun;20(2):329–341. doi: 10.1016/0092-8674(80)90619-4. [DOI] [PubMed] [Google Scholar]
  37. Miyamoto Y., Kuroda M., Munekata E., Masaki T. Stoichiometry of actin and phalloidin binding: one molecule of the toxin dominates two actin subunits. J Biochem. 1986 Dec;100(6):1677–1680. doi: 10.1093/oxfordjournals.jbchem.a121877. [DOI] [PubMed] [Google Scholar]
  38. Morris A., Tannenbaum J. Cytochalasin D does not produce net depolymerization of actin filaments in HEp-2 cells. Nature. 1980 Oct 16;287(5783):637–639. doi: 10.1038/287637a0. [DOI] [PubMed] [Google Scholar]
  39. Neidl C., Engel J. Exchange of ADP, ATP and 1: N6-ethenoadenosine 5'-triphosphate at G-actin. Equilibrium and kinetics. Eur J Biochem. 1979 Nov 1;101(1):163–169. doi: 10.1111/j.1432-1033.1979.tb04228.x. [DOI] [PubMed] [Google Scholar]
  40. Ornelles D. A., Fey E. G., Penman S. Cytochalasin releases mRNA from the cytoskeletal framework and inhibits protein synthesis. Mol Cell Biol. 1986 May;6(5):1650–1662. doi: 10.1128/mcb.6.5.1650. [DOI] [PMC free article] [PubMed] [Google Scholar]
  41. Pantaloni D., Carlier M. F., Coué M., Lal A. A., Brenner S. L., Korn E. D. The critical concentration of actin in the presence of ATP increases with the number concentration of filaments and approaches the critical concentration of actin.ADP. J Biol Chem. 1984 May 25;259(10):6274–6283. [PubMed] [Google Scholar]
  42. Rampal A. L., Pinkofsky H. B., Jung C. Y. Structure of cytochalasins and cytochalasin B binding sites in human erythrocyte membranes. Biochemistry. 1980 Feb 19;19(4):679–683. doi: 10.1021/bi00545a011. [DOI] [PubMed] [Google Scholar]
  43. Ravdin J. I., Guerrant R. L., Sperelakis N. Entamoeba histolytica: impedance measurements and cytotoxicity in the presence of bepridil, verapamil, and cytochalasin D. Exp Parasitol. 1985 Aug;60(1):63–72. doi: 10.1016/s0014-4894(85)80023-0. [DOI] [PubMed] [Google Scholar]
  44. Schliwa M. Action of cytochalasin D on cytoskeletal networks. J Cell Biol. 1982 Jan;92(1):79–91. doi: 10.1083/jcb.92.1.79. [DOI] [PMC free article] [PubMed] [Google Scholar]
  45. Tellam R., Frieden C. Cytochalasin D and platelet gelsolin accelerate actin polymer formation. A model for regulation of the extent of actin polymer formation in vivo. Biochemistry. 1982 Jun 22;21(13):3207–3214. doi: 10.1021/bi00256a027. [DOI] [PubMed] [Google Scholar]
  46. Tilney L. G., Inoué S. Acrosomal reaction of Thyone sperm. II. The kinetics and possible mechanism of acrosomal process elongation. J Cell Biol. 1982 Jun;93(3):820–827. doi: 10.1083/jcb.93.3.820. [DOI] [PMC free article] [PubMed] [Google Scholar]
  47. Wang Y. L. Exchange of actin subunits at the leading edge of living fibroblasts: possible role of treadmilling. J Cell Biol. 1985 Aug;101(2):597–602. doi: 10.1083/jcb.101.2.597. [DOI] [PMC free article] [PubMed] [Google Scholar]
  48. Wehland J., Osborn M., Weber K. Phalloidin-induced actin polymerization in the cytoplasm of cultured cells interferes with cell locomotion and growth. Proc Natl Acad Sci U S A. 1977 Dec;74(12):5613–5617. doi: 10.1073/pnas.74.12.5613. [DOI] [PMC free article] [PubMed] [Google Scholar]
  49. Wehland J., Weber K. Actin rearrangement in living cells revealed by microinjection of a fluorescent phalloidin derivative. Eur J Cell Biol. 1981 Jun;24(2):176–183. [PubMed] [Google Scholar]
  50. Wieland T., Faulstich H. Amatoxins, phallotoxins, phallolysin, and antamanide: the biologically active components of poisonous Amanita mushrooms. CRC Crit Rev Biochem. 1978 Dec;5(3):185–260. doi: 10.3109/10409237809149870. [DOI] [PubMed] [Google Scholar]
  51. Wieland T., de Vries J. X., Schäfer A., Faulstich H. Spectroscopic evidence for the interaction of phalloidin with actin. FEBS Lett. 1975 Jun 1;54(1):73–75. doi: 10.1016/0014-5793(75)81071-4. [DOI] [PubMed] [Google Scholar]
  52. Wulf E., Deboben A., Bautz F. A., Faulstich H., Wieland T. Fluorescent phallotoxin, a tool for the visualization of cellular actin. Proc Natl Acad Sci U S A. 1979 Sep;76(9):4498–4502. doi: 10.1073/pnas.76.9.4498. [DOI] [PMC free article] [PubMed] [Google Scholar]
  53. Yahara I., Harada F., Sekita S., Yoshihira K., Natori S. Correlation between effects of 24 different cytochalasins on cellular structures and cellular events and those on actin in vitro. J Cell Biol. 1982 Jan;92(1):69–78. doi: 10.1083/jcb.92.1.69. [DOI] [PMC free article] [PubMed] [Google Scholar]
  54. Yanagida T., Nakase M., Nishiyama K., Oosawa F. Direct observation of motion of single F-actin filaments in the presence of myosin. Nature. 1984 Jan 5;307(5946):58–60. doi: 10.1038/307058a0. [DOI] [PubMed] [Google Scholar]

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