Search tips
Search criteria 


Logo of jcellbiolHomeThe Rockefeller University PressEditorsContactInstructions for AuthorsThis issue
J Cell Biol. 1987 October 1; 105(4): 1473–1478.
PMCID: PMC2114638

Effects of cytochalasin and phalloidin on actin

Full Text

The Full Text of this article is available as a PDF (840K).

Selected References

These references are in PubMed. This may not be the complete list of references from this article.
  • Barden JA, Miki M, Hambly BD, Dos Remedios CG. Localization of the phalloidin and nucleotide-binding sites on actin. Eur J Biochem. 1987 Feb 2;162(3):583–588. [PubMed]
  • Bonder EM, Fishkind DJ, Mooseker MS. Direct measurement of critical concentrations and assembly rate constants at the two ends of an actin filament. Cell. 1983 Sep;34(2):491–501. [PubMed]
  • Bonder EM, Mooseker MS. 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. [PMC free article] [PubMed]
  • Bonder EM, Mooseker MS. 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. [PMC free article] [PubMed]
  • Bray D, Thomas C. Unpolymerized actin in fibroblasts and brain. J Mol Biol. 1976 Aug 25;105(4):527–544. [PubMed]
  • Brenner SL, Korn ED. 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]
  • 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]
  • Carlier MF, Criquet P, Pantaloni D, Korn ED. 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]
  • Casella JF, Flanagan MD, 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. [PubMed]
  • Coluccio LM, Tilney LG. Phalloidin enhances actin assembly by preventing monomer dissociation. J Cell Biol. 1984 Aug;99(2):529–535. [PMC free article] [PubMed]
  • Cooper JA, Bryan J, Schwab B, 3rd, Frieden C, Loftus DJ, Elson EL. Microinjection of gelsolin into living cells. J Cell Biol. 1987 Mar;104(3):491–501. [PMC free article] [PubMed]
  • Coué M, Korn ED. 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]
  • Dancker P, Löw I. Complex influence of cytochalasin B on actin polymerization. Z Naturforsch C. 1979 Aug;34(7-8):555–557. [PubMed]
  • 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. [PubMed]
  • Detmers PA, Goodenough UW, 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. [PMC free article] [PubMed]
  • Estes JE, Selden LA, Gershman LC. Mechanism of action of phalloidin on the polymerization of muscle actin. Biochemistry. 1981 Feb 17;20(4):708–712. [PubMed]
  • Faulstich H, Schäfer AJ, Weckauf M. The dissociation of the phalloidin-actin complex. Hoppe Seylers Z Physiol Chem. 1977 Feb;358(2):181–184. [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]
  • Fox JE, Phillips DR. Inhibition of actin polymerization in blood platelets by cytochalasins. Nature. 1981 Aug 13;292(5824):650–652. [PubMed]
  • 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. [PubMed]
  • Füchtbauer A, Jockusch BM, Maruta H, Kilimann MW, Isenberg G. Disruption of microfilament organization after injection of F-actin capping proteins into living tissue culture cells. Nature. 304(5924):361–364. [PubMed]
  • 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]
  • Goddette DW, Frieden C. The binding of cytochalasin D to monomeric actin. Biochem Biophys Res Commun. 1985 May 16;128(3):1087–1092. [PubMed]
  • Goddette DW, Frieden C. The kinetics of cytochalasin D binding to monomeric actin. J Biol Chem. 1986 Dec 5;261(34):15970–15973. [PubMed]
  • Goddette DW, Frieden C. Actin polymerization. The mechanism of action of cytochalasin D. J Biol Chem. 1986 Dec 5;261(34):15974–15980. [PubMed]
  • Goddette DW, Uberbacher EC, Bunick GJ, Frieden C. Formation of actin dimers as studied by small angle neutron scattering. J Biol Chem. 1986 Feb 25;261(6):2605–2609. [PubMed]
  • Godman GC, Miranda AF. Cellular contractility and the visible effects of cytochalasin. Front Biol. 1978;46:277–429. [PubMed]
  • Harris HE, Weeds AG. Plasma gelsolin caps and severs actin filaments. FEBS Lett. 1984 Nov 19;177(2):184–188. [PubMed]
  • Hartwig JH, Stossel TP. Cytochalasin B and the structure of actin gels. J Mol Biol. 1979 Nov 5;134(3):539–553. [PubMed]
  • Howard TH, Oresajo CO. 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. [PMC free article] [PubMed]
  • Kirschner MW. Implications of treadmilling for the stability and polarity of actin and tubulin polymers in vivo. J Cell Biol. 1980 Jul;86(1):330–334. [PMC free article] [PubMed]
  • Lal AA, Korn ED. Reinvestigation of the inhibition of actin polymerization by profilin. J Biol Chem. 1985 Aug 25;260(18):10132–10138. [PubMed]
  • 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. [PubMed]
  • 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. [PubMed]
  • MacLean-Fletcher S, Pollard TD. Mechanism of action of cytochalasin B on actin. Cell. 1980 Jun;20(2):329–341. [PubMed]
  • 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. [PubMed]
  • 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. [PubMed]
  • 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. [PubMed]
  • Ornelles DA, Fey EG, Penman S. Cytochalasin releases mRNA from the cytoskeletal framework and inhibits protein synthesis. Mol Cell Biol. 1986 May;6(5):1650–1662. [PMC free article] [PubMed]
  • Pantaloni D, Carlier MF, Coué M, Lal AA, Brenner SL, Korn ED. 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]
  • Rampal AL, Pinkofsky HB, Jung CY. Structure of cytochalasins and cytochalasin B binding sites in human erythrocyte membranes. Biochemistry. 1980 Feb 19;19(4):679–683. [PubMed]
  • Ravdin JI, Guerrant RL, 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. [PubMed]
  • Schliwa M. Action of cytochalasin D on cytoskeletal networks. J Cell Biol. 1982 Jan;92(1):79–91. [PMC free article] [PubMed]
  • 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. [PubMed]
  • Tilney LG, 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. [PMC free article] [PubMed]
  • Wang YL. Exchange of actin subunits at the leading edge of living fibroblasts: possible role of treadmilling. J Cell Biol. 1985 Aug;101(2):597–602. [PMC free article] [PubMed]
  • 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. [PubMed]
  • 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]
  • 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. [PubMed]
  • Wieland T, de Vries JX, Schäfer A, Faulstich H. Spectroscopic evidence for the interaction of phalloidin with actin. FEBS Lett. 1975 Jun 1;54(1):73–75. [PubMed]
  • Wulf E, Deboben A, Bautz FA, 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. [PubMed]
  • 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. [PMC free article] [PubMed]
  • 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. [PubMed]

Articles from The Journal of Cell Biology are provided here courtesy of The Rockefeller University Press