Inhibition of phosphatidylinositol 4,5-bisphosphate-stimulated phospholipase D2 activity by Ser/Thr phosphorylation

Biochim Biophys Acta. 2000 Feb 2;1495(2):121-4. doi: 10.1016/s0167-4889(99)00165-2.

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