1. Regulation of phospholipase C-delta by GTP-binding proteins-rhoA as an inhibitory modulator
- Author
-
Joanne S Lymn, Christopher C. Ashley, Alun D. Hughes, and Elizabeth A.M. Hodson
- Subjects
RHOA ,Botulinum Toxins ,G protein ,Antidotes ,GTPgammaS ,Guanosine ,GTP-binding protein ,Chemical Fractionation ,Deferoxamine ,Sulfur Radioisotopes ,GTP Phosphohydrolases ,chemistry.chemical_compound ,Phospholipase C delta ,GTP-binding protein regulators ,Adenosine Triphosphate ,GTP-Binding Proteins ,Animals ,Molecular Biology ,Exoenzyme C3 ,ADP Ribose Transferases ,Adenosine Diphosphate Ribose ,Phospholipase C ,biology ,Guanosine 5'-O-(3-Thiotriphosphate) ,RhoA ,Cell Biology ,Molecular biology ,Phospholipase Cδ1 ,Enzyme Activation ,Isoenzymes ,chemistry ,Biochemistry ,Type C Phospholipases ,biology.protein ,Sodium Fluoride ,Cattle ,rhoA GTP-Binding Protein - Abstract
The regulation of Phospholipase C (PLC)delta activity remains obscure. These studies show that PLCdelta1 activity is significantly enhanced by both guanosine thiotriphosphate (GTPgammaS) and Clostridium botulinum exoenzyme C3 (C3) but not by aluminium fluoride. C3 ADP ribosylated a 21-kDa protein in the PLCdelta1 preparation and Western blotting identified rhoA in these samples. RhoA acts as an inhibitory modulator of PLCdelta activity.
- Published
- 1998