SYNAPTOTAGMIN IS ENDOGENOUSLY PHOSPHORYLATED BY CA-2+ CALMODULIN PROTEIN KINASE-II IN SYNAPTIC VESICLES

The cytoplasmic domain of synaptotagmin (a synaptic vesicle-specific protein) has a high degree of homology with the Ca2+-phospholipid binding domain of protein kinase C. The Ca2+-phospholipid binding activity of synaptotagmin has been implicated in the docking and fusion of synaptic vesicles with the presynaptic membrane during Ca2+-induced exocytosis. The protein sequence contains potential phosphorylation sites for various protein kinases which could modulate its binding activity. At present there is no clear evidence that the protein is endogenously phosphorylated in intact vesicles. Here it is reported that phospho-synaptotagmin was immunoprecipitated from endogenously phosphorylated synaptic vesicles. The conditions used indicate that synaptotagmin, as synapsin I, is phosphorylated by Ca2+/calmodulin-dependent protein kinase II