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Phalloidin

Phalloidin is  a toxin from the toadstool "Death Cap" (Amanita phalloides) that binds actin (Löw & Wieland 1974).  Binding is specific for F-actin and this has provided a very convenient tool to study this distribution of F-actin in permeabilised cells since fluorescent analogs can be synthesized that retain actin binding (Wulf et al, 1979). Phalloidin binds to actin at the junction between subunits (Barden et al, 1987; Faulstich et al, 1993; Steinmetz et al, 1998) and because this is not a site at which many actin-binding proteins bind, most of the F-actin in cells is available for phalloidin labelling.  There are two notable exceptions, these being nebulin and ADF/cofilins.  Nebulin is an unusual actin binding protein in that each molecule binds about as 200 actin monomers within the thin filament of muscle.  The actin binding site seems to compete directly with the nebulin-binding repeat (Ao & Lehrer, 1995).  The ADF/cofilin group alter the twist of the actin filament so that the junction between the monomers is altered in such a manner as to be no longer suitable for phalloidin binding.  The ADF/Cofilins therefore appear to compete indirectly with phalloidin for binding.  Gelsolin may act likewise as they share a similar fold to ADF/cofilins and also seems to compete for phalloidin binding (Allen & Janmey, 1994).
References:-

Adami, R., Choquet, D. & Grazi, E. (1999) Rhodamine phalloidin F-actin. Critical concentration versus tensile strength.  Eur.J.Biochem. 263, 270-275.

Akiyama, T. & Matsumoto, J. (1984) Microinjection studies of the effects of anti-actin antibody, phalloidin and DNase-1 on pigment migration in swordtail erythrophores. Yale Journal Of Biology And Medicine. 57, 331.

Allen, P. G. & Janmey, P. A. (1994) Gelsolin displaces phalloidin from actin filaments.  J. Biol. Chem. 269, 32916-32923.

Allen, P. G., Shuster, C. B., Käs, J., Chaponnier, C., Janmey, P. A. & Herman, I. M. (1996) Phalloidin binding and rheological differences among actin isoforms. Biochemistry. 35, 14062-14069.

Ao, X. & Lehrer, S. S. (1995) Phalloidin unzips nebulin from thin filaments in skeletal myofibrils. J.Cell Sci. 108, 3397-3403.

Ballweber, E., Hannappel, E., Niggemeyer, B. & Mannherz, H. G. (1994) Induction of the polymerization of actin from the actin:thymosin b4 complex by phalloidin, skeletal myosin subfragment 1, chicken intestinal myosin I and free ends of filamentous actin.  Eur. J. Biochem. 223, 419-426.

Barden, J. A., Miki, M., Hambly, B. D. & dos Remedios, C. G. (1987) Localization of the phalloidin and nucleotide-binding sites on actin.  Eur.J.Biochem. 162, 583-588.

Bar-Ziv, R., Tlusty, T., Moses, E., Safran, S. A. & Bershadsky, A. (1999) Pearling in cells: A clue to understanding cell shape. PNAS. 96, 10140-10145.

Bubb, M. R., Senderowicz, A. M. J., Sausville, E. A., Duncan, K. L. K. & Korn, E. D. (1994) Jasplakinolide, a cytotoxic natural product, induces actin polymerization and competitively inhibits the binding of phalloidin to F-actin. J. Biol. Chem. 269, 14869-14871.

Bubb, M. R., Spector, I., Breshadsky, A. D. & Korn, E. D. (1995) Swinholide A is a microfilament disrupting marine toxin that stabilizes actin dimers and severs actin filaments. J. Biol. Chem. 270, 3463-3466.

Capani, F., Deerinck, T. J., Ellisman, M. H., Bushong, E., Bobik, M. & Martone, M. E. (2001) Phalloidin-eosin followed by photo-oxidation: A novel method for localizing F-actin at the light and electron microscope levels.  J. Histochem.Cytochem. 49, 1351-1361.

Cooper, J. A. (1987) Effects of cytochalasin and phalloidin on actin.  J.Cell Biol. 105, 1473-1478.

Danker, P., Löw, I., Hasselbach, W. & Wieland, T. (1975) Interaction of actin with phalloidin: Polymerization and stabilization of F-actin. Biochim.Biophys. Acta. 400, 407-414.

De La Cruz, E. M. & Pollard, T. (1996) Kinetics and thermodynamics of phalloidin binding to actin filaments from three divergent species. Biochemistry. 35, 14054-14061.

De La Cruz, E. M. & Pollard, T. D. (1994) Transient kinetic analysis of rhodamine phalloidin binding to actin filaments. Biochemistry. 33, 14387-14392.

Doris, F. P. & Steer, M. W. (1996) Effects of fixatives and permeabilisation buffers on pollen tubes: implications for localisation of actin microfilaments using phalloidin staining.  Protoplasma. 195, 25-36.

Drubin, D. G., Jones, H. D. & Wertman, K. F. (1993) Actin structure and function: Roles in mitochondrial organization and morphogenesis in budding yeast and identification of the phalloidin-binding site.  Mol.Biol.Cell. 4, 1277-1294.

Estes, J. E., Selden, L. A. & Gershman, L. C. (1981) Mechanism of action of phalloidin on the polymerization of muscle actin. Biochemistry. 20, 708-712.

Faulstich, H., Zobeley, S., Heintz, D. & Drewes, G. (1993) Probing the phalloidin binding site of actin. FEBS Letters. 318, 218-222.

Freyburger, G., Belloc, F. & Boisseau, M. R. (1990) Flow cytometry analysis of human neutrophils labeled with rhodamine phalloidin: Effect of Pentoxyfylline. Biorheology. 27, 445-448.

Goddette, D. W. & Frieden, C. (1986) The kinetics of cytochalasinD binding to monomeric actin.  J.Biol.Chem. 261, 15970-15973.

Goddette, D. W. & Frieden, C. (1986) Actin polymerization. The mechanism of action of cytochalasin D. J.Biol.Chem. 261, 15974-15980.

Gronewold, T. M. A., Sasse, F., Lündsdorf, H. & Reichenbach, H. (1999) Effects of rhizopodin and latrunculin B on the morphology and on the actin cytoskeleton of mammalian cells. Cell Tissue Research. 295, 121-129.

Joos, L. & Gicquad, C. (1986) Effect of phalloidin and viroisin on Acanthamoeba castellanii after permeabilization of the cell.  Biochem.Cell Biol. 65, 261-270.

Kinosian, H. J., Selden, L. A., Estes, J. E. & Gershman, L. C. (1996) Kinetics of gelsolin interaction with phalloidin-stabilized F-actin. Rate constants for binding and severing. Biochemistry. 35, 16550-16556.

Kinosian, H. J., Seldon, L. A., Estes, J. E. & Gershman, L. G. (1993) Actin filament annealing in the presence of ATP and phalloidin. Biochemistry. 32, 12353-12357.

LeBihan, T. & Gicquaud, C. (1991) Stabilization of actin by phalloidin: a differential scanning calorimetric study. Biochem.Biophys.Res.Comm. 181, 542-547.

Löw, I., Danker, P. & Wieland, T. (1976) Stabilization of actin polymer structure by phalloidin: ATPase activity of actin induced by phalloidin at low pH. FEBS letters. 65, 358-360.

Löw, I. & Wieland, T. (1974) The interaction of phalloidin, some of its derivatives, and other cyclic peptides with muscle actin as studied by viscometry. FEBS letters. 44, 340-343.

Miki, M. (1987) The recovery of polymerizability of Lys-61-labelled actin by the addition of phalloidin. Eur.J.Biochem. 164, 229-235.

Miki, M., Barden, J. A., dos Remedios, C. G., Philips, L. & Hambly, B. D. (1987) Interaction of phalloidin with chemically modified actin. Eur.J.Biochem. 165, 125-130.

Moens, P. D. J., Yee, D. J. & dos Remedios, C. G. (1994) Determination of the radial coordinate of Cys-374 in F-actin using fluorescence resonance energy transfer spectroscopy: effect of phalloidin on polymer assembly. Biochemistry. 33, 13102-13108.

Mozo-Villarias, A. & Ware, B. R. (1984) Distinctions between mechanisms of cytchalasin D activity for Mg2+-and K+-induced actin assembly.  J.Biol.Chem. 259, 5549-5554.

Ohmori, H., Toyama, S. & Toyama, S. (1992) Direct proof that the primary site of action of cytochalasin on cell motility processes is actin. J. Cell Biol. 116, 933-941.

Pinaev, G., Schutt, C. E. & Lindberg, U. (1995) The effect on actin ATPase of phalloidin and tetramethylrhodamine phalloidin. FEBS Lett. 369, 144-148.

Saito, S., Watabe, S., Ozaki, H., Kigoshi, H., Yamada, K., Fusetani, N. & Karaki, H. (1996) Novel actin depolymerizing macrolide Aplyronine A  J.Biochem. 120, 552-555.

Sampath, P. & Pollard, T. D. (1991) Effects of cytochalasin, phalloidin and pH on the elongation of actin filaments. Biochemistry. 30, 1973-1980.

Schäfer, A., De Vries, J. X., Faulstich, H. & Wieland, T. (1975) Phalloidin counteracts the inhibitory effect of actin on deoxyribonuclease 1.  FEBS letters. 57, 51-53.

Small, J. V., Zobeley, S., Rinnerthaler, G. & Faulstich, H. (1988) Coumarin-phalloidin; a new actin probe permitting triple immunofluorescence microscopy of the cytoskeleton. J.Cell Sci. 89, 21-24.

Steinmetz, M. O., Stoffler, D., Müller, S. A., Jahn, W., Wolpensinger, B., Goldie, K. N., Engel, A., Faulstich, H. & Aebi, U. (1998) Evaluating atomic models of F-actin with an undecagold-tagged phalloidin derivative. J.Mol.Biol. 276, 1-6.

Toyama, S. & Toyama, S. (1988) Functional alterations in b'-actin from a KB cell mutant resistant to cytochalasin B.  J.Cell Biol. 107, 1499-1504.

Wendel, H. & Dancker, P. (1986) Kinetics of actin polymerization: influence of ions, temperature, age of F-actin, cytochalsin B and phalloidin. Biochim.Biophys.Acta. 873, 387-396.

Wendel, H. & Dancker, P. (1987) Influence of phalloidin on both the nucleation and the elongation phase of actin polymerization. Biochim.Biophys.Acta. 915, 199-204.

Wulf, E., Deboben, A., Bautz, F. A., Faulstich, H. & Wieland, T. H. (1979) Fluorescent phallotoxin, a tool for the visualization of cellular actin. Proc.Nat.Acad.Sci.USA. 76, 4498-4502.

Zhukarev, V., Sanger, J. M., Sanger, J. W., Goldman, Y. E. & Shuman, H. (1997) Distribution and orientation of rhodamine-phalloidin bound to thin filaments in skeletal and cardiac myofibrils. Cell Mot.Cytoskel. 37, 363-377.

 
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