Cyclic AMP‐dependent protein kinase stimulates the formation of polyphosphoinositides in lymphocyte plasma membrane

Abstract

Inside-out vesicles from lymphocyte plasma membrane were phosphorylated in the presence of [γ-³²P]ATP. The dissociated catalytic subunit of cyclic AMP-dependent protein kinase stimulated both membrane protein and membrane lipid phosphorylation, indicating the presence of a phosphorylation cascade. The phosphorylated membrane lipids were analyzed by thin-layer chromatography. Increase of ³²P-labelling stimulated by the cyclic AMP-dependent protein kinase was found exclusively in polyphosphoinositides.