New aspects of neurotransmitter release and exocytosis: dynamic and differential regulation of synapsin I phosphorylation by acute neuronal excitation in vivo.

Synapsin I is a synaptic vesicle-associated protein that is phosphorylated at multiple sites by various protein kinases. It has been proposed to play an important role in the regulation of neurotransmitter release and the organization of cytoskeletal architecture in the presynaptic terminal. In the present minireview, I describe the dynamic changes in synapsin I phosphorylation induced by acute neuronal excitation in vivo, and discuss its regulation by protein kinases and phosphatases and its functional significance in vivo. When acute neuronal excitation was induced by electroconvulsive treatment (ECT) in rats, phosphorylation of synapsin I at multiple sites was decreased during brief seizure activity in hippocampal and parieto-cortical homogenates. After termination of the seizure activity, phosphorylation at mitogen-activated protein kinase-dependent sites was increased dramatically. Phosphorylation at a Ca(2+)/calmodulin-dependent protein kinase II-dependent site was also increased moderately afterwards. The dynamic and differential changes in synapsin I phosphorylation induced by acute neuronal excitation may be involved in plastic changes induced by ECT and may have some role in its effectiveness for the treatment of psychiatric diseases in humans.