Entrapment of Rho ADP-ribosylated by Clostridium botulinum C3 exoenzyme in the Rho-guanine nucleotide dissociation inhibitor-1 complex.

@article{Genth2003EntrapmentOR,
  title={Entrapment of Rho ADP-ribosylated by Clostridium botulinum C3 exoenzyme in the Rho-guanine nucleotide dissociation inhibitor-1 complex.},
  author={Harald Genth and Ralf Gerhard and Akio Maeda and Mutsuki Amano and Kozo Kaibuchi and Klaus Aktories and Ingo Just},
  journal={The Journal of biological chemistry},
  year={2003},
  volume={278 31},
  pages={28523-7}
}
RhoA, -B, and -C are ADP-ribosylated by Clostridium botulinum exoenzyme C3 to induce redistribution of the actin filaments in intact cells, a finding that has led to the notion that the ADP-ribosylation blocks coupling of Rho to the downstream effectors. ADP-ribosylation, however, does not alter nucleotide binding, intrinsic, and GTPase-activating protein-stimulated GTPase activity. ADP-ribosylated Rho is even capable of activating the effector protein ROK in a recombinant system. Treatment of… CONTINUE READING

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