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J. Biol. Chem., Vol. 269, Issue 42, 25951-25954, Oct, 1994
KC Malcolm, AH Ross, RG Qiu, M Symons and JH Exton
Stimulation of phospholipase D by guanosine 5'-O-(3-thiotriphosphate) (GTP
gamma S) in rat liver plasma membranes indicates the involvement of
GTP-binding proteins. We used RhoGDI, an inhibitor of GDP dissociation from
small GTP-binding proteins of the Rho family, to determine the involvement
of these proteins. Incubation, and subsequent washing, of plasma membranes
with RhoGDI dose-dependently diminished GTP gamma S-stimulated
phospholipase D activity, as determined by accumulation of
phosphatidylethanol in the presence of ethanol. Incubation with RhoGDI also
caused a rapid and dose-dependent appearance of RhoA in the wash, which was
associated with the inhibition of phospholipase D. RhoGDI also rapidly
extracted Cdc42 from membranes, but Rac1 was not extracted. Full
reconstitution of GTP gamma S-stimulated phospholipase D in RhoGDI-washed
membranes was achieved with recombinant RhoA. There was partial
reconstitution with Rac1 and no enhancement with Cdc42 or ADP-ribosylation
factor. The response to RhoA was dose-dependent (EC50 = 0.5 microM).
ADP-ribosylation of RhoA by Clostridium botulinum C3 exoenzyme did not
affect its ability to recover GTP gamma S-stimulated phospholipase D
activity in RhoGDI- washed membranes. These findings support a role for
GTP-binding proteins of the Rho family in the activation of
membrane-associated phospholipase D and implicate RhoA as the major protein
involved.
Activation of rat liver phospholipase D by the small GTP-binding protein RhoA
Howard Hughes Medical Institute, Nashville, Tennessee.
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