Activation of rat liver phospholipase D by the small GTP-binding protein RhoA.
作者： K C Malcolm , A H Ross , R G Qiu , M Symons , J H Exton
DOI: 10.1016/S0021-9258(18)47140-2
关键词:
摘要: Stimulation of phospholipase D by guanosine 5'-O-(3-thiotriphosphate) (GTP gamma S) in rat liver plasma membranes indicates the involvement GTP-binding proteins. We used RhoGDI, an inhibitor GDP dissociation from small proteins Rho family, to determine these Incubation, and subsequent washing, with RhoGDI dose-dependently diminished GTP S-stimulated activity, as determined accumulation phosphatidylethanol presence ethanol. Incubation also caused a rapid dose-dependent appearance RhoA wash, which was associated inhibition D. rapidly extracted Cdc42 membranes, but Rac1 not extracted. Full reconstitution RhoGDI-washed achieved recombinant RhoA. There partial no enhancement or ADP-ribosylation factor. The response (EC50 = 0.5 microM). Clostridium botulinum C3 exoenzyme did affect its ability recover activity membranes. These findings support role for family activation membrane-associated implicate major protein involved.
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