| Background | Synapsin I plays a key role in synaptic plasticity in brain (Feng et al., 2002; Nayak et al., 1996). This effect is due in large part to the ability of the synapsins to regulate the availability of synaptic vesicles for release. In addition to its role in plasticity, the expression of synapsin I is a precise indicator of synapse formation (Moore and Bernstein, 1989; Stone et al., 1994). Thus, synapsin I immunocytochemistry provides a valuable tool for the study of synaptogenesis. The role of synapsin in synaptic plasticity and in synaptogensis is regulated by phosphorylation (Jovanovic et al., 2001; Kao et al., 2002). Serine 9 is the site on synapsin I that is phosphorylated by cAMP-dependent protein kinase and by calcium calmodulin kinase I (Czernik et al., 1987). Phosphorylation of this site is thought to Western blot of rat cortical lysate showing specific regulate synaptic vesicle function and neurite outgrowth (Kao et al., immunolabeling of the ~78 kDa synapsin I phosphorylated at 9 2002). Ser in the first lane (-). Phosphospecificity is shown in the second lane (+) where the immunolabeling is completely eliminated by blot treatment with lambda phosphatase ( Lambda- |
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