ADP-ribosylation of actin

Adler, K. B., Krill, J., Alberghini, T. V. &Evans, J. N. (1983) Effect of cytochalasin D on smooth muscle contraction.Cell Motil. 3, 545–51.PubMedGoogle Scholar

Aktories, K., Bärmann, M., Ohishi, I., Tsuyama, S., Jakobs, K. H. &Habermann, E. (1986) Botulinum C2 toxin ADP-ribosylates actin.Nature 322, 390–2.PubMedGoogle Scholar

Althaus, F. R. &Richter, C. (1987) ADP-ribosylation of proteins. Enzymology and biological significance. (edited bySolioz, M.) pp. 1–237 Springer-Verlag Berlin Heidelberg, New York.Google Scholar

Geipel, U., Just, I., Schering, B., Haas, D. &Aktories, K. (1989) ADP-ribosylation of actin causes increase in the rate of ATP exchange and inhibition of ATP hydrolysis.Eur. J. Biochem. 179, 229–32.PubMedGoogle Scholar

Geipel, U., Just, T. &Aktories, K. (1990) Inhibition of cyclochalasin D-stimulated G-actin ATPase by ADP-ribosylation withClostridium perfringeus iota toxin.Biochem. J. 266, 335–9.PubMedGoogle Scholar

Jacquemin, C., Thibout, H., Lambert, B. &Correze, C. (1986) Endogenous ADP-ribosylation of G_s subunit and autonomous regulation of adenylate cyclase.Nature 323, 182–4.PubMedGoogle Scholar

Just, I., Geipel, U. &Aktories, K. (1989) ADP-ribosylation of actin by clostridial toxins: reversible inhibition of actin ATPase.Naunyn Schmiedeberg's Arch. Pharmacol. Suppl. III Vol340, R72.Google Scholar

Lee, H. &Iglewski, W. J. (1984) Cellular ADP-ribosylation with the same mechanism of actin as diphtheria toxin andPseudomonas toxin A.Proc. Natl. Acad. Sci. USA 81, 2703–7.PubMedGoogle Scholar

Mauss, S., Koch, G., Kreye, V. A. W. &Aktories, K. (1989) Inhibition of the contraction of the isolated longitudinal muscle of the guinea pig ileum by botulinum C2 toxin: evidence for a role of G/F-actin transition in smooth muscle contraction.Naunyn-Schmiedeherg's Arch. Pharmacol. 340, 345–51.Google Scholar

Norgauer, J., Kownatzki, E., Seifert, R. &Aktories, K. (1988) Botulinum C2 toxin ADP-ribosylates actin and enhances O₂⁻ production and secretion but inhibits migration of activated human neutrophils.J. Clin. Invest. 82, 1376–82.PubMedGoogle Scholar

Norgauer, J., Just, I., Aktories, K. &Sklar, L. A. (1989) Influence of Botulinum C2 toxin on F-actin and N-formyl peptide receptor dynamics in human neutrophils.J. Cell Biol. 109, 1133–40.PubMedGoogle Scholar

Ohishi, I. &Miyake, M. (1985) Biniding of two components of C2 toxin to epithelial cells and brush borders of mouse intestine.Infect. Immun. 48, 769–75.PubMedGoogle Scholar

Popoff, M. R., Rubin, E. J., Gill, D. M. &Boquet, P. (1988) Actin-specific ADP-ribosyltransferase produced by aClostridium difficile strain.Infect. Immun. 56, 2299–306.PubMedGoogle Scholar

Reuner, K. H., Presek, P., Boscheck, C. B. &Aktories, K. (1987) Botulinum C2 toxin ADP-ribosylates actin and disorganizes the microfilament network in intact cells.Eur. J. Cell Biol. 43, 134–40.PubMedGoogle Scholar

Schering, B., Bärmann, M., Chhatwal, G. S., Geipel, U., &Aktories, K. (1988) ADP-ribosylation of skeletal muscle and non-muscle actin byClostridium perfringens iota toxin.Eur. J. Biochem. 171, 225–9.PubMedGoogle Scholar

Simpson, L. L., Stiles, B. G., Zepeda, H. &Wilkins, T. D. (1989) Production byClostridium spiroforme of an iotalike toxin that possesses mono(ADP-ribosyl)transferase activity: identification of a novel class of ADP-ribosyltransferases.Infect. Immun. 57, 225–61.PubMedGoogle Scholar

Tanuma, S., Kawashima, K. &Endo, H. (1988) Eukaryotic mono(ADP-ribosyl)transferases that ADP-ribosylates GTP-binding regulatory G₁ protein.J. Biol. Chem. 263, 5485–89.PubMedGoogle Scholar

Vendekerckhove, J., Schering, B., Bärmann, M., &Aktories, K. (1988) Botulinum C2 toxin ADP-ribosylates cytoplasmicβ/γ-actin in arginine 177.J. Biol. Chem. 263, 696–700.PubMedGoogle Scholar

Wegner, A. &Aktories, K. (1988) ADP-ribosylated actin caps the barbed ends of actin filaments.J. Biol. Chem. 263, 13739–42.PubMedGoogle Scholar