Phosphorylation of elongation factor 2 in the rat superior cervical ganglion.

Elongation factor 2 (EF-2) and its associated kinase, Ca2+/calmodulin-dependent protein kinase III, have recently been identified as a major protein phosphorylation system in mammalian tissues. We have measured the phosphorylation of EF-2 in 32P-labeled superior cervical ganglia. Phosphorylation of EF-2 was increased by preganglionic stimulation or by treatment of the ganglion with dimethylphenylpiperazinium or veratridine. Increases in EF-2 phosphorylation presumably reflect the activation of Ca2+/calmodulin-dependent protein kinase III by nicotinic stimulation and depolarization. The phosphorylation of EF-2 may help to coordinate neuronal protein synthesis with neuronal activity.