Cyclic AMP-dependent protein kinase stimulates the formation of polyphosphoinositides in lymphocyte plasma membrane.
Inside-out vesicles from lymphocyte plasma membrane were phosphorylated in the presence of [gamma -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.
D002384:Catalysis; D002462:Cell Membrane / Q000378:metabolism; D000242:Cyclic AMP / Q000097:blood; D006801:Humans; D066298:In Vitro Techniques; D007700:Kinetics; D008055:Lipids / Q000097:blood; D008214:Lymphocytes / Q000378:metabolism* / Q000648:ultrastructure; D010716:Phosphatidylinositols / Q000096:biosynthesis*; D010766:Phosphorylation; D011494:Protein Kinases / Q000097:blood*
D008055:Lipids; D010716:Phosphatidylinositols; D000242:Cyclic AMP; D011494:Protein Kinases