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Vol. 8, Issue 12, 2437-2447, December 1997
*Departments of Molecular Physiology and Biological Physics,
Pathology and Internal Medicine, University of Virginia Health Sciences
Center, Charlottesville, Virginia 22906-0011; and
Pretreatment of intact rabbit portal vein smooth muscle with the
chimeric toxin DC3B (10INSERM
U452, Faculte de Medicine, Nice 06107, Cedex 2, France
6 M, 48 h; ; ) ADP-ribosylated endogenous RhoA, including cytosolic RhoA complexed with rhoGDI, and
inhibited the tonic phase of phenylephrine-induced contraction and the
Ca2+-sensitization of force by phenylephrine, endothelin
and guanosine triphosphate (GTP)
S, but did not inhibit
Ca2+-sensitization by phorbol dibutyrate. DC3B also
inhibited GTPS-induced translocation of cytosolic RhoA () to the membrane fraction. In DC3B-treated
muscles the small fraction of membrane-associated RhoA could be
immunoprecipitated, even after exposure to GTPS, which prevents
immunoprecipitation of non-ADP-ribosylated RhoA. Dissociation of
cytosolic RhoA-rhoGDI complexes with SDS restored the
immunoprecipitability and ADP ribosylatability of RhoA, indicating that
both the ADP-ribosylation site (Asn 41) and RhoA insert loop () are masked by rhoGDI and that the long
axes of the two proteins are in parallel in the heterodimer. We
conclude that RhoA plays a significant role in G-protein-, but not
protein kinase C-mediated, Ca2+ sensitization and that ADP
ribosylation inhibits in vivo the Ca2+-sensitizing effect
of RhoA by interfering with its binding to a membrane-associated
effector.
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