Abstract
Treatment of HeLa cells overexpressing PLD2 with the Ser/Thr-specific protein phosphatase inhibitor, okadaic acid, augmented spontaneous phosphorylation of PLD2 with concomitant inhibition of phosphatidylinositol 4,5-bisphosphate (PIP(2))-stimulated PLD2 activity. Dephosphorylation of the immunoprecipitated, spontaneously phosphorylated PLD2 in COS-7 cells by catalytic subunit of protein phosphatase 1gamma1 resulted in the stimulation of the PLD2 catalytic activity. These observations suggest that Ser/Thr phosphorylation regulates PLD2 activity.
Publication types
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Animals
-
COS Cells
-
Enzyme Inhibitors / pharmacology
-
HeLa Cells
-
Humans
-
Okadaic Acid / pharmacology
-
Phosphatidylinositol 4,5-Diphosphate / antagonists & inhibitors
-
Phosphatidylinositol 4,5-Diphosphate / pharmacology*
-
Phospholipase D / antagonists & inhibitors*
-
Phospholipase D / biosynthesis
-
Phospholipase D / chemistry
-
Phosphorylation
-
Serine / chemistry
-
Threonine / chemistry
-
Transfection
Substances
-
Enzyme Inhibitors
-
Phosphatidylinositol 4,5-Diphosphate
-
Okadaic Acid
-
Threonine
-
Serine
-
phospholipase D2
-
Phospholipase D