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J. Biol. Chem., Vol. 278, Issue 31, 28523-28527, August 1, 2003

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Entrapment of Rho ADP-ribosylated by Clostridium botulinum C3 Exoenzyme in the Rho-Guanine Nucleotide Dissociation Inhibitor-1 Complex^*

Harald Genth  , Ralf Gerhard , Akio Maeda ¶, Mutsuki Amano ¶, Kozo Kaibuchi ¶, Klaus Aktories || and Ingo Just 

From the Institut für Toxikologie, Medizinische Hochschule D-30625 Hannover, Germany, the ^||Institut für experimentelle und klinische Pharmakologie und Toxikologie der Universität Freiburg, D-79098 Freiburg, Germany, and the ^¶Department of Cell Pharmacology, Nagoya University Graduate School of Medicine, Nagoya 466-8550, Japan

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 cells with a cell-permeable chimeric C3 toxin led to complete localization of modified Rho to the cytosolic fraction based on the complexation of ADP-ribosylated Rho with the guanine-nucleotide dissociation inhibitor-1 (GDI-1). The modified complex turned out to be resistant to phosphatidylinositol 4,5-bisphosphate- and GTPS-induced release of Rho from GDI-1. Thus, ADP-ribosylation leads to entrapment of Rho in the GDI-1 complex. The increased stability of the GDI complex prevented binding of Rho to membrane-associated players of the GTPase cycle such as the activating guanine nucleotide exchange factors and effector proteins.

Received for publication, February 24, 2003

^* This work was supported by Deutsche Forschungsgemeinschaft Project Ju231/3 and Sonder forschungsbereich 388. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

To whom correspondence should be addressed: Institut für Toxikologie, Medizinische Hochschule Hannover, Carl-Neuberg-Str. 1, D-30625 Hannover, Germany. Tel.: 49-511-532-2807; Fax: 49-511-532-2879; E-mail: genth.harald{at}mh-hannover.de.

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