Synapsin I is expressed in epithelial cells: localization to a unique trans-Golgi compartment.

@article{Bustos2001SynapsinII,
  title={Synapsin I is expressed in epithelial cells: localization to a unique trans-Golgi compartment.},
  author={Rodrigo Bustos and Esther Kolen and Lita Braiterman and Anthony J. Baines and Fred S. Gorelick and Ann L. Hubbard},
  journal={Journal of cell science},
  year={2001},
  volume={114 Pt 20},
  pages={3695-704}
}
Synapsin I is abundant in neural tissues. Its phosphorylation is thought to regulate synaptic vesicle exocytosis in the pre-synaptic terminal by mediating vesicle tethering to the cytoskeleton. Using anti-synapsin antibodies, we detected an 85 kDa protein in liver cells and identified it as synapsin I. Like brain synapsin I, non-neuronal synapsin I is phosphorylated in vitro by protein kinase A and yields identical (32)P-peptide maps after limited proteolysis. We also detected synapsin I mRNA… CONTINUE READING
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