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J. Biol. Chem., Vol. 268, Issue 30, 22251-22254, Oct, 1993
J Zhang, WG King, S Dillon, A Hall, L Feig and SE Rittenhouse
The small GTP-binding protein Rho regulates the assembly of actin stress
fibers and focal adhesions in cells responding to growth factors.
ADP-ribosylation of Rho by C3 transferase blocks this function; however, an
enzymatic target for Rho has not yet been defined. We now report that Rho
activates phosphatidylinositide 3- kinase in soluble preparations of
platelets. Activation of phosphatidylinositide 3-kinase by GTP gamma S is
blocked by ADP- ribosylation of endogenous Rho, and Rho shifts to the
cytoskeleton in platelets exposed to thrombin. The inhibitory effects of
ADP- ribosylation are overcome by exogenous recombinant Rho but not by
recombinant Rac, another member of the Ras superfamily. Exposure of
platelets to thrombin has been reported to lead to activation of
phosphatidylinositide 3-kinase, a shift of this enzyme to the platelet
membrane skeleton, and rapid cytoskeletal reorganization. In other studies,
ADP-ribosylation of Rho has been found to inhibit thrombin- induced
platelet aggregation, a cytoskeletally linked event. We suggest that Rho
may exert its effects on cytoskeletal reorganization via
phosphatidylinositide 3-kinase.
Activation of platelet phosphatidylinositide 3-kinase requires the small GTP-binding protein Rho
Department of Pharmacology/Jefferson Cancer Institute, Thomas Jefferson University, Philadelphia, Pennsylvania.
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