Inhibition of phosphatidylinositol 4,5-bisphosphate-stimulated phospholipase D2 activity by Ser/Thr phosphorylation.
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.
Watanabe
H
H
Department of Biological Information, Tokyo Institute of Technology, Nagatsuta, Midori-ku, Yokohama, Japan.
Kanaho
Y
Y
D000818:Animals; D019556:COS Cells; D004791:Enzyme Inhibitors / Q000494:pharmacology; D006367:HeLa Cells; D006801:Humans; D019319:Okadaic Acid / Q000494:pharmacology; D019269:Phosphatidylinositol 4,5-Diphosphate / Q000037:antagonists & inhibitors / Q000494:pharmacology*; D010739:Phospholipase D / Q000037:antagonists & inhibitors* / Q000096:biosynthesis / Q000737:chemistry; D010766:Phosphorylation; D012694:Serine / Q000737:chemistry; D013912:Threonine / Q000737:chemistry; D014162:Transfection
D004791:Enzyme Inhibitors; D019269:Phosphatidylinositol 4,5-Diphosphate; D019319:Okadaic Acid; D013912:Threonine; D012694:Serine; C105606:phospholipase D2; D010739:Phospholipase D