Cyclic AMP-dependent protein kinase and Ca2+-calmodulin stimulate the formation of polyphosphoinositides in a sarcoplasmic reticulum preparation of rabbit heart. 
A rabbit heart membrane fraction enriched in sarcoplasmic reticulum was incubated in a reaction mixture containing [gamma-32P]ATP.  The catalytic subunit of cyclic AMP-dependent protein kinase enhanced the 32P-labelling of both phosphatidylinositol-4-phosphate and phosphatidylinositol-4,5-bisphosphate.  Ca2 +-calmodulin also increased the 32P-incorporation into both polyphosphoinositides.  Upon SDS gel-electrophoretic analysis of the membrane proteins, phospholamban was found to be concurrently phosphorylated by the exogenous catalytic subunit as well as by an endogenous Ca2+-calmodulin-dependent protein kinase.