Probing nucleation, cutting and capping of actin filaments

Andrea Gaertner1, Klaus Ruhnau1, Elke Schröer1, Norma Selve1, Michael Wanger1, Albrecht Wegner1
1Institute of Physiological Chemistry, Ruhr-University Bochum, Bochum F.R.G.

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Bonder, E. M., Fishkind, D. J. &Mooseker, M. S. (1983) Direct measurement of critical concentration and assembly rate constants at two ends of an actin filament.Cell 34, 491–501. Bonder, E. M. &Mooseker, M. S. (1983) Direct electron microscopic visualization of barbed end capping and filament cutting by intestinal microvillar 95-kdalton protein (villin): A new actin assembly assay using theLimulus acrosomal process.J. Cell. Biol. 96, 1097–107. Carlier, M.-F., Pantaloni, D. &Korn, E. D. (1984) Evidence for an ATP cap at the ends of actin filaments and its regulation of the F-actin steady state.J. Biol. Chem. 259, 9983–6. Chaponnier, C., Patebex, P. &Gabbiani, G. (1985) Human plasma actin-depolymerizing factor: Purification, biological activity and localization in leukocytes and platelets.Eur. J. Biochem. 146, 267–76. Colombo, R. &Milzani, A. (1988) How does doxorubicin interfere with actin polymerization?Biochim. Biophys. Acta 968, 9–16 Coluccio, L. M., Sedlar, P. A. &Bryan, J. (1986) The effects of a 45000 molecular weight protein from unfertilized sea urchin eggs and its 1∶1 actin complex on actin filaments.J. Muscle Res.Cell Mot. 7, 133–41. Cooper, J. A., Blum, J. D., Williams, R. C. &Pollard, T. D. (1986) Purification and characterization of actophorin, a new 15000-dalton actin-binding protein fromAcanthamoeba castelanii.J. Biol. Chem. 261, 477–85. Cooper, J. A. &Pollard, T. D. (1985) Effect of capping protein on the kinetics of actin polymerization.Biochemistry,24, 793–9. Coué, M. &Korn, E. D. (1985) Interaction of plasma gelsolin with G-actin and F-actin in the presence and absence of calcium ions.J. Biol. Chem. 260, 15033–41. Craig, S. W. &Powell, L. D. (1980) Regulation of actin polymerization by villin, a 95000 dalton cytoskeletal component of intestinal brush borders.Cell,22, 739–46. Detmers, P., Weber, A., Elzinga, M. &Stephens, R. E. (1981) 7-Chloro-4-nitro-2-oxa-1,3-diazole actin as a probe for actin polymerization.J. Biol. Chem. 256, 99–105. Frieden, C. (1985) Actin and tubulin polymerization: The use of kinetic methods to determine mechanism.Ann. Rev. Biophys. Chem. 14, 189–210. Glenney, J. R., Kaulfus, P. &Weber, K. (1981) F-actin assembly modulated by villin: Ca2+-dependent nucleation and capping of the barbed end.Cell,24, 471–80. Grazi, E. (1985) Polymerization of N-(1-pyrenyl)-iodoacetamide-labeled actin: The fluorescence signal is not directly proportional to the incorporation of the monomer into the polymer.Biochem. Biophys. Res. Comm. 128, 1058–63. Grazi, E., Trombetta, G. &Magri, E. (1984) A mechanism for the selective preservation of homogeneous F(ATP) actin.Biochem. Int. 9, 669–74. Harris, H. E. &Weeds, A. G. (1983) Plasma actin depolymerizing factor has both calcium-dependent and calcium-independent effects on actin.Biochemistry,22, 2728–41. Harris, H. E. &Weeds, A. G. (1984) Plasma gelsolin caps and severs actin filaments.FEBS Lett. 177, 184–8. Hasegawa, T., Takahashi, S., Hayashi, H. &Hatano, S. (1980) Fragmin: A calcium ion sensitive regulatory factor on the formation of actin filaments.Biochemistry 19, 2677–83. Hinssen, H. (1981a) An actin-modulating protein fromPhysarum polycephalum. I. Isolation and purification.Eur. J. Cell. Biol. 23, 225–33. Hinssen, H. (1981b) An actin-modulating protein fromPhysarum polycephalum. II. Ca2+-dependence and other properties.Eur. J. Cell Biol. 23, 234–40. Hosoya, H. &Mabuchi, I. (1984) A 45000-mol-Wt protein-actin complex from unfertilized sea urchin egg affects assembly properties of actin.J. Cell Biol. 99, 994–1001. Hosoya, H., Mabuchi, I. &Sakai, H. (1986) An 100kDa Ca2+-sensitive actin-fragmenting protein from unfertilized sea urchin egg.Eur. J. Biochem. 154, 233–9. Isenberg, G., Aebi, U. &Pollard, T. D. (1980) An actin-binding protein fromAcanthamoeba regulates actin filament polymerization and interactions.Nature, Lond. 288, 455–9. Janmey, P. A., Chaponnier, C., Lind, S. E., Zaner, K. S., Stossel, T. P. &Yin, H. L. (1985) Interactions of geloslin and gelsolin-actin complexes with actin. Effects of calcium on actin nucleation, filament severing, and end blocking.Biochemistry,24, 3714–23. Kondo, H. &Ishiwata, S. (1976) Uni-directional growth of F-actin.J. Biochem., Tokyo 79, 159–71. Korn, E. D. (1982) Actin polymerization and its regulation by proteins from nonmuscle cells.Physiol. Rev.,62, 672–737. Kouyama, T. &Mihashi, K. (1981) Fluorimetry Study of N-(1-pyrenyl)iodoacetamide-labelled F-actin. Local structural change of actin protomer both on polymerization and on binding of heavy meromyosin.Eur. J. Biochem. 114, 33–8. Kurth, M. C., Wang, L.-L., Dingus, J. &Bryan, J. (1983) Purification and characterization of a gelsolin-actin complex from human platelets.J. Biol. Chem. 258, 10895–903. Lal, A. A., Korn, E. D. &Brenner, S. L. (1984) Rate constants for actin polymerization in ATP determined using cross-linked actin trimers as nuclei.J. Biol. Chem. 259, 8794–800. Lees, A., Haddad, J. G. &Lin, S. (1984) Brevin and vitamin D binding protein: Comparison of the effects of two serum proteins on actin assembly and disassembly.Biochemistry 23, 3038–47. Martin, F., Derancourt, J., Capony, J.-P., Watrin, A. &Cavadore, J.-C. (1988) A 36 kDa monomeric protein and its complex with a 10 kDa protein both isolated from bovine aorta are calpactin-like proteins that differ in their Ca2+-dependent calmodulin-binding and actin-severing properties.Biochem. J. 251, 777–85. Maruta, H. &Isenberg, G. (1983) Ca2+-dependent actin-binding phosphoprotein inPhysarum polycephalum. II. Ca2+-dependent F-actin-capping activity of subunit a and its regulation by phosphorylation of subunit b.J. Biol. Chem. 258, 10151–8. Maruyama, K., Kimura, S., Ishii, T., Kuroda, M., Ohashi, K. &Muramatsa, S. (1977) β-actinin, a regulatory protein of muscle.J. Biochem., Tokyo 81, 215–32. Mooseker, M. S., Graves, T. A., Wharton, K. A., Falco, N. &Howe, C. L. (1980) Regulation of microvillus structure: Calcium-dependent solation and cross-linking of actin filaments in the microvilli of intestinal epithelial cells.J. Cell Biol. 87, 809–22. Neuhaus, J.-M., Wanger, M., Reiser, T. &Wegner, A. (1983) Treadmilling of actin.J. Muscle Res. Cell Mot. 4, 507–27. Nishida, R., Maekawa, S., Muneyuki, E. &Sakai, H. (1984) Action of a 19K protein from porcine brain on actin polymerization: A new functional class of actin-binding proteins.J. Biochem., Tokyo 95, 387–98. Norberg, R., Thorstensson, R., Utter, G. &Fagraeus, A. (1979) F-actin-depolymerizing activity of human serum.Eur. J. Biochem. 100, 575–83. Olomucki, A., Huc., C., Lefébure, F. &Coué, M. (1984) Isolation and characterization of human blood platelet gelsolin.FEBS Lett. 174, 80–5. Oosawa, F. &Kasai, M. (1962) A theory of linear and helical aggregation of marcromolecules.J. Mol. Biol. 4, 10–21. Oosawa, M., Shimaoka, S., Funatsu, T., Ishiwata, S. &Maruyama, K. (1987) β-actinin is not distinguishable from actin barbed-end capping protein in chicken breast muscle.J. Biochem., Tokyo 101, 1481–3. Pinder, J. C., Weeds, A. G. &Gratzer, W. B. (1986) Study of actin filament ends in the human red cell membrane.J. Mol. Biol. 191, 461–8. Pollard, T. D. (1986) Rate constants for the reaction of ATP- and ADP-actin with the ends of actin filaments.J. Cell Biol. 103, 2747–54. Pollard, T. D. &Cooper, J. A. (1986) Actin and actin-binding proteins. A critical evaluation of mechanisms and functions.Ann. Rev. Biochem. 55, 987–1035. Pollard, T. D. &Mooseker, M. S. (1981) Direct measurement of actin polymerization rate constants by electron microscopy of actin. Filaments nucleated by isolated microvillus cores.J. Cell Biol. 88, 654–9. Porte, F. &Harricane, M.-C. (1986) Interactions of plasma gelsolin with actin. Isolation and characterization of binary and ternary plasma-gelsolin-actin complexes.Eur. J. Biochem. 154, 87–93. Rickard, J. E. &Sheterline, P. (1986) Cytoplasmic concentrations of inorganic phosphate affect the critical concentration for assembly of actin in the presence of cytochalasin D or ADP.J. Mol. Biol.,191, 273–80. Ruhnau, K., Schröer, E. &Wegner, A. (1988) Characterization of the actin polymerization-inhibiting protein from chicken gizzard smooth muscle.Eur. J. Biochem. 170, 583–7. Schröer, E. &Wegner, A. (1985) Purification and characterization of a protein from chicken gizzard, which inhibits actin polymerization.Eur. J. Biochem,153, 515–20. Selve, N. &Wegner, A. (1986a) Rate of treadmillingin vitro.J. Mol. Biol. 187, 627–31. Selve, N. &Wegner, A. (1986b) Rate constant for capping of the barbed ends of actin filaments by the gelsolinactin complex.Eur. J. Biochem. 155, 397–401. Selve, N. &Wegner, A. (1986c) Rate constants and equilibrium constants for binding of the gelsolin-actin complex to the barbed ends of actin filaments in the presence and absence of calcium.Eur. J. Biochem. 160, 379–87. Southwick, F. S. &Dinubile, M. J. (1986) Rabbit alveolar macrophages contain Ca2+-sensitive, 41,000-dalton protein which reversibly blocks the ‘barbed’ ends of actin filaments but does not sever them.J. Biol. Chem. 261, 14191–5. Tellam, R. &Frieden, C. (1982) Cytochalasin D and platelet gelsolin accelerate actin polymer formation. A model for regulation of the extent of actin polymer formationin vivo.Biochemistry 21, 3207–14. Walsh, T. P., Weber, A., Davis, K., Bonder, E. &Mooseker, M. S. (1984a) Calcium dependence of villin-induced actin depolymerization.Biochemistry 23, 6099–102. Walsh, T. P., Weber, A., Higgins, J., Bonder, E. M. &Mooseker, M. S. (1984b) Effect of villin on the kinetics of actin polymerization.Biochemistry 23, 2613–21. Wanger, M. &Wegner, A. (1985) Equilibrium constant for binding of an actin filament capping protein to the barbed end of actin filaments.Biochemistry 24, 1035–40. Weber, A., Northrop, J., Bishop, M. F., Ferrone, F. A. &Mooseker, M. S. (1987) Kinetics of actin elongation and depolymerization at the pointed ends.Biochemistry 26, 2537–44. Wegner, A. (1976) Head to tail polymerization of actin.J. Mol. Biol. 108, 139–50. Wegner, A. &Aktories, K. (1988) ADP-ribosylated actin caps the barbed ends of actin filaments.J. Biol. Chem. 263, 13739–42. Wegner, A. &Engel, J. (1975) Kinetics of the cooperative association of actin to actin filaments.Biophys. Chem. 3, 215–25. Wegner, A. &Isenberg, G. (1983) 12-fold difference between the critical monomer concentrations of the two ends of actin filaments in physiological salt conditions.Proc. Natl. Acad. Sci. USA 80, 4922–5. Wilkins, J. A. &Lin, S. (1982) High-affinity interaction of vinculin with actin filamentsin vitro.Cell 28, 83–90. Yamamoto, K., Pardee, J. D., Reidler, J., Stryer, L. &Spudich, J. A. (1982) Mechanism of interaction ofDictyostelium severin with actin filaments.J. Cell Biol. 95, 711–9. Yin, H. L., Hartwig, J. H., Maruyama, K. &Stossel, T. P. (1981) Ca2+ control of actin filament length. Effects of macrophage gelsolin on actin polymerization.J. Biol. Chem. 256, 9693–7. Yin, H. L. &Stossel, T. P. (1979) Control of cytoplasmic actin in gel-sol transformation by gelsolin, a calcium-dependent regulatory protein.Nature, Lond. 281, 583–6.