Characteristics of Ca2+/calmodulin- and Ca2+/phosphatidylserine-stimulated phosphoproteins in rat striatum.

The characteristics of endogenous Ca2+/calmodulin (CaM)- and Ca2+/phosphatidylserine (PS)-stimulated phosphorylated proteins in the striatum of rat were partially determined and compared in this study. The Ca2+/CaM-dependent phosphoproteins were associated with serine and threonine residues. The sensitivity of these proteins for phosphorylation by Ca2+/CaM was not affected by pretreatment of tissue with Ca2+ chelating agent, EGTA or with non-ionic detergent, Triton X-114. Triton X-114 phase separation experiments revealed that these Ca2+/CaM-dependent phosphoproteins were partitioned in the detergent rich phase suggesting that they are integral proteins of the striatal membrane. On the other hand, the Ca2+/PS-dependent phosphorylated proteins were primarily associated with the serine residue. Phosphorylation of these proteins by Ca2+/PS were abolished after the treatment with EGTA or Triton X-114. These results suggest that Ca2+/PS-dependent striatal phosphoproteins are biochemically unstable in maintaining their state of phosphorylation.