Enhanced phospholipase D activity and altered morphology in RhoA-overexpressing RAT1 fibroblasts.
Small GTP-binding proteins of the Rho family are implicated in the regulation of phospholipase D (PLD). However, few studies have addressed their role in agonist-stimulated PLD activity in vivo. Stable lines of Rat1 fibroblasts overexpressing RhoA were shown to have altered morphology. Moreover, they demonstrated increased PLD activity when stimulated with lysophosphatidic acid, platelet-derived growth factor, and phorbol ester, compared with vector-transfected cells. However, phosphoinositide phospholipase C activity was unaltered by overexpression of RhoA. These data indicate a critical downstream role for RhoA in agonist-stimulated PLD activity in intact cells.
Malcolm
K C
KC
Howard Hughes Medical Institute, Vanderbilt University School of Medicine, Nashville, Tennessee 37221, USA.
Sable
C L
CL
Elliott
C M
CM
Exton
J H
JH
D000818:Animals; D002460:Cell Line; D004789:Enzyme Activation; D005347:Fibroblasts / Q000201:enzymology / Q000378:metabolism; D019204:GTP-Binding Proteins / Q000235:genetics* / Q000378:metabolism; D010739:Phospholipase D / Q000378:metabolism*; D051381:Rats; D010738:Type C Phospholipases / Q000378:metabolism; D020742:rhoA GTP-Binding Protein
D010738:Type C Phospholipases; D010739:Phospholipase D; D019204:GTP-Binding Proteins; D020742:rhoA GTP-Binding Protein