Synapsin
I is a member of the synapsin gene family. Synapsins encode
neuronal phosphoproteins which associate with the cytoplasmic
surface of synaptic vesicles. Family members are characterized
by common protein domains, and they are implicated in synaptogenesis
and the modulation of neurotransmitter release, suggesting
a potential role in several neuropsychiatric diseases.
This member of the synapsin family plays a role in regulation
of axonogenesis and synaptogenesis. The protein serves
as a substrate for several different protein kinases and
phosphorylation may function in the regulation of this
protein in the nerve terminal.
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.
Serine 9 is the site on synapsin I that is phosphorylated
by cAMP-dependent protein kinase and by calcium calmodulin
kinase I. Phosphorylation of this site is thought to regulate
synaptic vesicle function. |